Nuclear Hsp104 safeguards the dormant translation machinery during quiescence

The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated...

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Published inNature communications Vol. 15; no. 1; pp. 315 - 20
Main Authors Kohler, Verena, Kohler, Andreas, Berglund, Lisa Larsson, Hao, Xinxin, Gersing, Sarah, Imhof, Axel, Nyström, Thomas, Höög, Johanna L., Ott, Martin, Andréasson, Claes, Büttner, Sabrina
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 05.01.2024
Nature Publishing Group
Nature Portfolio
Subjects
14
14/19
14/28
42/35
45/47
631/337/574
631/45/470/2284
631/80/470/2284
631/80/642/1363
82/58
96/63
Aging
Biosynthesis
Cell and Molecular Biology
Cell Cycle
Cell Division
Cell viability
Cell- och molekylärbiologi
Cytosol
Heat-Shock Proteins - metabolism
Humanities and Social Sciences
Initiation factor eIF-2
Metabolism
multidisciplinary
Nuclei (cytology)
Nutrients
Protein Aggregates
Protein Biosynthesis
Protein folding
Protein interaction
Protein synthesis
Proteins
Proteomes
Quality control
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Science
Science (multidisciplinary)
Yeast
Online AccessGet full text
ISSN2041-1723
2041-1723
DOI10.1038/s41467-023-44538-8

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Abstract The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished. During aging, proteins are damaged and can misfold, compromising cellular viability. Here, Kohler et al. uncover how aging cells maintain fitness by redirecting the protein repair factor Hsp104 to the nucleus in response to metabolic cues.
AbstractList The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished. During aging, proteins are damaged and can misfold, compromising cellular viability. Here, Kohler et al. uncover how aging cells maintain fitness by redirecting the protein repair factor Hsp104 to the nucleus in response to metabolic cues.
The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.
The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.
Abstract The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.
The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality control compartment that handles misfolded proteins produced by the cytosolic protein biosynthesis system. Here, we find that age-associated metabolic cues target the yeast protein disaggregase Hsp104 to the nucleus to maintain a functional nuclear proteome during quiescence. The switch to respiratory metabolism and the accompanying decrease in translation rates direct cytosolic Hsp104 to the nucleus to interact with latent translation initiation factor eIF2 and to suppress protein aggregation. Hindering Hsp104 from entering the nucleus in quiescent cells results in delayed re-entry into the cell cycle due to compromised resumption of protein synthesis. In sum, we report that cytosolic-nuclear partitioning of the Hsp104 disaggregase is a critical mechanism to protect the latent protein synthesis machinery during quiescence in yeast, ensuring the rapid restart of translation once nutrients are replenished.During aging, proteins are damaged and can misfold, compromising cellular viability. Here, Kohler et al. uncover how aging cells maintain fitness by redirecting the protein repair factor Hsp104 to the nucleus in response to metabolic cues.
ArticleNumber 315
Author Andréasson, Claes
Büttner, Sabrina
Imhof, Axel
Nyström, Thomas
Höög, Johanna L.
Kohler, Andreas
Ott, Martin
Hao, Xinxin
Kohler, Verena
Berglund, Lisa Larsson
Gersing, Sarah
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crossref_primary_10_1083_jcb_202407123
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Cites_doi 10.1016/j.jmb.2019.04.014
10.1038/nature02026
10.1016/j.sbi.2018.12.004
10.1016/S0092-8674(00)80830-2
10.7554/eLife.65484
10.1073/pnas.1913207117
10.1126/science.aac4354
10.1126/science.1216242
10.7554/eLife.34532
10.1126/science.1091317
10.1038/nmeth.2019
10.1016/j.molcel.2018.01.004
10.1073/pnas.1719398115
10.1038/nature10317
10.1134/S0006297921120105
10.1515/hsz-2020-0187
10.7554/eLife.18638
10.1083/jcb.201201074
10.1128/MCB.00027-17
10.1016/j.biochi.2020.12.017
10.1379/CSC-31.1
10.1016/j.cell.2022.11.001
10.1021/acs.jproteome.8b00702
10.1002/yea.3681
10.1016/S0092-8674(00)81223-4
10.1093/femsyr/fow027
10.1002/1873-3468.13844
10.1111/j.1365-2958.2008.06135.x
10.1126/science.2188365
10.1016/j.tcb.2016.05.004
10.1038/s41598-019-41060-0
10.1016/j.str.2012.01.006
10.1002/j.1460-2075.1992.tb05295.x
10.1007/s002840010251
10.1083/jcb.201612018
10.1080/10409238.2016.1230087
10.1002/iub.1597
10.1016/j.molcel.2021.12.031
10.2174/0929866528666211125114421
10.1016/j.tibs.2018.02.003
10.1093/hmg/ddq089
10.1046/j.1365-2958.2001.02339.x
10.3389/fmolb.2022.1106477
10.1002/yea.3155
10.1128/jb.176.18.5802-5813.1994
10.1002/yea.1142
10.1021/bi0493766
10.1021/cb200308e
10.1083/jcb.148.4.635
10.1016/j.cub.2013.09.058
10.1371/journal.pbio.1001346
10.1126/science.aan1052
10.1016/j.csbj.2022.08.033
10.1016/j.molcel.2020.07.024
10.1002/bip.21301
10.1038/nm.4001
10.1101/gad.5.12a.2315
10.1016/j.molcel.2013.01.020
10.1002/yea.3545
10.1101/cshperspect.a034066
10.1016/j.molcel.2016.05.014
10.3389/fmolb.2023.1155521
10.1126/science.aaw9157
10.1126/science.1065810
10.1093/emboj/cdg362
10.1093/emboj/18.3.754
10.18632/aging.100613
10.1021/acs.jproteome.7b00913
10.1042/BCJ20190584
10.1073/pnas.1921890117
10.1016/j.molcel.2019.09.014
10.15252/embj.201489524
10.7554/eLife.18413
10.1021/acs.biochem.5b00801
10.1042/BST0360120
10.1091/mbc.E21-01-0014
10.1038/nchembio.304
10.1128/MCB.21.22.7569-7575.2001
10.1002/pmic.201700108
10.1038/s41580-019-0101-y
10.1038/nrm2993
10.1021/acs.biochem.1c00052
10.1091/mbc.e10-12-1007
10.1016/j.celrep.2020.107680
10.1093/nar/gkh033
10.1074/mcp.M114.046995
10.1016/j.ymeth.2017.04.020
10.1016/j.jbc.2022.102199
10.1007/978-3-030-38266-7_4
10.1046/j.1365-2958.2002.02860.x
10.1146/annurev.biochem.70.1.603
10.1016/j.jsb.2003.10.009
10.1006/jsbi.1996.0013
10.1038/nprot.2007.13
10.1101/cshperspect.a034033
10.1016/j.celrep.2020.108637
10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N
10.1242/jcs.213025
10.1016/j.chembiol.2010.12.010
10.15252/embj.2022111802
10.7554/eLife.56525
10.1016/j.mcpro.2023.100552
10.1038/s41556-023-01128-6
10.1242/jcs.179648
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References Hipp, Kasturi, Hartl (CR3) 2019; 20
den Brave, Engelke, Becker (CR89) 2021; 478
Borgert, Mishra, den Brave (CR46) 2022; 20
Sun, Gresham (CR16) 2021; 38
Krishnamurthy (CR55) 2011; 6
Solís (CR75) 2016; 63
Scheufler (CR80) 2000; 101
Doncheva, Morris, Gorodkin, Jensen (CR99) 2019; 18
Assimon, Southworth, Gestwicki (CR78) 2015; 54
Schneider-Poetsch (CR58) 2010; 6
Christie (CR104) 2004; 32
Peters, Karmon, Miodownik, Ben-Aroya (CR26) 2016; 129
Stumpf (CR53) 2010; 19
Zeytuni, Zarivach (CR84) 2012; 20
Wheeler, Matheny, Jain, Abrisch, Parker (CR21) 2016; 5
Youn (CR24) 2019; 76
Tosal-Castano (CR95) 2021; 34
Miller (CR47) 2015; 34
Fuge, Braun, Werner-Washburne (CR57) 1994; 176
Kohler, Andréasson (CR4) 2023; 10
Pechmann, Willmund, Frydman (CR70) 2013; 49
Zakariya, Zehra, Khan (CR13) 2022; 29
CR45
Gates (CR40) 2017; 357
Mathew (CR65) 2017; 216
Marshall, Vierstra (CR25) 2018; 7
Winkler, Tyedmers, Bukau, Mogk (CR60) 2012; 198
Jawed (CR31) 2022; 9
Balchin, Hayer-Hartl, Hartl (CR8) 2016; 353
Rajoo, Vallotton, Onischenko, Weis (CR52) 2018; 115
Blatch, Lässle (CR87) 1999; 21
Das, Mukherjee, Bedi, Ghosh (CR54) 2021; 86
Prodromou (CR77) 1999; 18
Kohler, Andréasson (CR12) 2020; 401
Sagot, Laporte (CR17) 2019; 132
Chang (CR61) 2011; 18
Sanchez, Lindquist (CR43) 1990; 248
Joutsen, Sistonen (CR5) 2019; 11
Nillegoda, Wentink, Bukau (CR29) 2018; 43
Masser, Kandasamy, Kaimal, Andréasson (CR100) 2016; 33
Duennwald, Echeverria, Shorter (CR64) 2012; 10
Grimminger-Marquardt, Lashuel (CR86) 2010; 93
Coller (CR15) 2011; 334
Smith (CR85) 2004; 9
CR69
Frydman (CR67) 2001; 70
Tong (CR98) 2001; 294
Moggridge, Sorensen, Morin, Hughes (CR102) 2018; 17
Gietz, Schiestl (CR91) 2007; 2
Araujo (CR79) 2021; 182
Savitski, Wilhelm, Hahne, Kuster, Bantscheff (CR103) 2015; 14
Singh (CR101) 2020; 79
Mogk (CR32) 2004; 146
Tye, Churchman (CR74) 2021; 32
Hartl, Bracher, Hayer-Hartl (CR2) 2011; 475
López-Otín, Blasco, Partridge, Serrano, Kroemer (CR11) 2023; 186
Grousl, Vojtova, Hasek, Vomastek (CR18) 2022; 39
Protter, Parker (CR19) 2016; 26
Mogk, Haslberger, Tessarz, Bukau (CR30) 2008; 36
Basisty, Meyer, Schilling (CR6) 2018; 18
Frottin (CR48) 2019; 365
Arpalahti, Haglund, Holmberg (CR10) 2020; 1233
Amorós, Estruch (CR36) 2001; 39
Grably, Stanhill, Tell, Engelberg (CR37) 2002; 44
den Brave (CR63) 2020; 31
Jung, Masison (CR59) 2001; 43
Bitran, Jacobs, Zhai, Shakhnovich (CR68) 2020; 117
Perez-Riba, Itzhaki (CR88) 2019; 54
Tessarz, Mogk, Bukau (CR33) 2008; 68
Janke (CR92) 2004; 21
Kaimal, Kandasamy, Gasser, Andréasson (CR62) 2017; 37
Kaushik, Cuervo (CR9) 2015; 21
Glover, Lindquist (CR41) 1998; 94
Sanchez, Taulien, Borkovich, Lindquist (CR39) 1992; 11
Wheeler, Jain, Khong, Parker (CR20) 2017; 126
Huh (CR49) 2003; 425
Dermouche, Chagot, Manival, Quinternet (CR81) 2021; 60
Choder (CR56) 1991; 5
Mosser, Ho, Glover (CR42) 2004; 43
Malcova, Farkasovsky, Senohrabkova, Vasicova, Hasek (CR93) 2016; 16
Brychzy (CR83) 2003; 22
Balchin, Hayer-Hartl, Hartl (CR7) 2020; 594
Mogk, Bukau, Kampinga (CR28) 2018; 69
Chamera (CR34) 2019; 431
Sadeh, Movshovich, Volokh, Gheber, Aharoni (CR38) 2011; 22
Schindelin (CR94) 2012; 9
Shorter, Southworth (CR35) 2019; 11
Cherkasov (CR14) 2013; 23
Radwan, Wood, Sui, Hatters (CR71) 2017; 69
Quintana-Gallardo (CR82) 2019; 9
Yedidi, Fatehi, Enenkel (CR27) 2016; 51
Kumar, Mathew, Stirling (CR44) 2022; 298
Kremer, Mastronarde, McIntosh (CR96) 1996; 116
Tyedmers, Mogk, Bukau (CR1) 2010; 11
Rout (CR51) 2000; 148
Andersson, Hanzén, Liu, Molin, Nyström (CR72) 2013; 5
Abbas-Terki, Donzé, Briand, Picard (CR50) 2001; 21
CR23
CR22
Nowicka (CR90) 2021; 10
Björkeroth (CR66) 2020; 117
Biebl (CR76) 2022; 82
Zheng (CR73) 2016; 5
Tong (CR97) 2004; 303
MR Grably (44538_CR37) 2002; 44
MP Rout (44538_CR51) 2000; 148
44538_CR23
44538_CR22
T Schneider-Poetsch (44538_CR58) 2010; 6
AHY Tong (44538_CR97) 2004; 303
S Sun (44538_CR16) 2021; 38
S Dermouche (44538_CR81) 2021; 60
SM Zakariya (44538_CR13) 2022; 29
SBM Miller (44538_CR47) 2015; 34
A Kumar (44538_CR44) 2022; 298
M Choder (44538_CR56) 1991; 5
I Malcova (44538_CR93) 2016; 16
W-K Huh (44538_CR49) 2003; 425
AE Masser (44538_CR100) 2016; 33
Y Sanchez (44538_CR43) 1990; 248
V Mathew (44538_CR65) 2017; 216
A Bitran (44538_CR68) 2020; 117
V Andersson (44538_CR72) 2013; 5
S Rajoo (44538_CR52) 2018; 115
M Amorós (44538_CR36) 2001; 39
L Quintana-Gallardo (44538_CR82) 2019; 9
EK Fuge (44538_CR57) 1994; 176
J Shorter (44538_CR35) 2019; 11
T Grousl (44538_CR18) 2022; 39
F den Brave (44538_CR63) 2020; 31
EJ Solís (44538_CR75) 2016; 63
C López-Otín (44538_CR11) 2023; 186
RD Gietz (44538_CR91) 2007; 2
RS Yedidi (44538_CR27) 2016; 51
44538_CR45
J-Y Youn (44538_CR24) 2019; 76
T Abbas-Terki (44538_CR50) 2001; 21
J Björkeroth (44538_CR66) 2020; 117
C Prodromou (44538_CR77) 1999; 18
V Kohler (44538_CR4) 2023; 10
L Arpalahti (44538_CR10) 2020; 1233
DSW Protter (44538_CR19) 2016; 26
DF Smith (44538_CR85) 2004; 9
MM Savitski (44538_CR103) 2015; 14
L Chang (44538_CR61) 2011; 18
X Zheng (44538_CR73) 2016; 5
A Sadeh (44538_CR38) 2011; 22
MM Biebl (44538_CR76) 2022; 82
A Jawed (44538_CR31) 2022; 9
ML Duennwald (44538_CR64) 2012; 10
V Kohler (44538_CR12) 2020; 401
A Mogk (44538_CR32) 2004; 146
SA Araujo (44538_CR79) 2021; 182
A Mogk (44538_CR30) 2008; 36
GL Blatch (44538_CR87) 1999; 21
NB Nillegoda (44538_CR29) 2018; 43
J Winkler (44538_CR60) 2012; 198
44538_CR69
T Chamera (44538_CR34) 2019; 431
S Kaushik (44538_CR9) 2015; 21
V Grimminger-Marquardt (44538_CR86) 2010; 93
Y Sanchez (44538_CR39) 1992; 11
JR Kremer (44538_CR96) 1996; 116
M Krishnamurthy (44538_CR55) 2011; 6
VA Assimon (44538_CR78) 2015; 54
A Perez-Riba (44538_CR88) 2019; 54
KR Christie (44538_CR104) 2004; 32
JD Stumpf (44538_CR53) 2010; 19
BW Tye (44538_CR74) 2021; 32
LZ Peters (44538_CR26) 2016; 129
D Balchin (44538_CR8) 2016; 353
NT Doncheva (44538_CR99) 2019; 18
J Frydman (44538_CR67) 2001; 70
L Borgert (44538_CR46) 2022; 20
RS Marshall (44538_CR25) 2018; 7
G Jung (44538_CR59) 2001; 43
JR Wheeler (44538_CR21) 2016; 5
S Moggridge (44538_CR102) 2018; 17
S Das (44538_CR54) 2021; 86
V Cherkasov (44538_CR14) 2013; 23
A Mogk (44538_CR28) 2018; 69
J Schindelin (44538_CR94) 2012; 9
F den Brave (44538_CR89) 2021; 478
C Janke (44538_CR92) 2004; 21
I Sagot (44538_CR17) 2019; 132
FU Hartl (44538_CR2) 2011; 475
D Balchin (44538_CR7) 2020; 594
S Pechmann (44538_CR70) 2013; 49
JR Glover (44538_CR41) 1998; 94
N Zeytuni (44538_CR84) 2012; 20
AP Singh (44538_CR101) 2020; 79
S Tosal-Castano (44538_CR95) 2021; 34
N Basisty (44538_CR6) 2018; 18
DD Mosser (44538_CR42) 2004; 43
A Brychzy (44538_CR83) 2003; 22
AHY Tong (44538_CR98) 2001; 294
M Radwan (44538_CR71) 2017; 69
JM Kaimal (44538_CR62) 2017; 37
C Scheufler (44538_CR80) 2000; 101
J Tyedmers (44538_CR1) 2010; 11
U Nowicka (44538_CR90) 2021; 10
F Frottin (44538_CR48) 2019; 365
J Joutsen (44538_CR5) 2019; 11
SN Gates (44538_CR40) 2017; 357
HA Coller (44538_CR15) 2011; 334
P Tessarz (44538_CR33) 2008; 68
MS Hipp (44538_CR3) 2019; 20
JR Wheeler (44538_CR20) 2017; 126
References_xml – volume: 431
  start-page: 2180
  year: 2019
  end-page: 2196
  ident: CR34
  article-title: Selective Hsp70-dependent docking of Hsp104 to protein aggregates protects the cell from the toxicity of the disaggregase
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2019.04.014
– ident: CR45
– ident: CR22
– volume: 425
  start-page: 686
  year: 2003
  end-page: 691
  ident: CR49
  article-title: Global analysis of protein localization in budding yeast
  publication-title: Nature
  doi: 10.1038/nature02026
– volume: 54
  start-page: 43
  year: 2019
  end-page: 49
  ident: CR88
  article-title: The tetratricopeptide-repeat motif is a versatile platform that enables diverse modes of molecular recognition
  publication-title: Current Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2018.12.004
– volume: 101
  start-page: 199
  year: 2000
  end-page: 210
  ident: CR80
  article-title: Structure of TPR domain–peptide complexes: critical elements in the assembly of the Hsp70–Hsp90 multichaperone machine
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80830-2
– volume: 10
  start-page: e65484
  year: 2021
  ident: CR90
  article-title: Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins
  publication-title: eLife
  doi: 10.7554/eLife.65484
– volume: 117
  start-page: 1485
  year: 2020
  end-page: 1495
  ident: CR68
  article-title: Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps
  publication-title: Proc. Natl Acad. Sci.
  doi: 10.1073/pnas.1913207117
– volume: 353
  start-page: aac4354
  year: 2016
  ident: CR8
  article-title: In vivo aspects of protein folding and quality control
  publication-title: Science
  doi: 10.1126/science.aac4354
– volume: 334
  start-page: 1074
  year: 2011
  end-page: 1075
  ident: CR15
  article-title: The essence of quiescence
  publication-title: Science
  doi: 10.1126/science.1216242
– volume: 7
  start-page: e34532
  year: 2018
  ident: CR25
  article-title: Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation
  publication-title: eLife
  doi: 10.7554/eLife.34532
– volume: 303
  start-page: 808
  year: 2004
  end-page: 813
  ident: CR97
  article-title: Global mapping of the yeast genetic interaction network
  publication-title: Science
  doi: 10.1126/science.1091317
– volume: 9
  start-page: 676
  year: 2012
  end-page: 682
  ident: CR94
  article-title: Fiji: an open-source platform for biological-image analysis
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2019
– volume: 69
  start-page: 214
  year: 2018
  end-page: 226
  ident: CR28
  article-title: Cellular handling of protein aggregates by disaggregation machines
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2018.01.004
– volume: 115
  start-page: E3969
  year: 2018
  end-page: E3977
  ident: CR52
  article-title: Stoichiometry and compositional plasticity of the yeast nuclear pore complex revealed by quantitative fluorescence microscopy
  publication-title: Proc. Natl Acad. Sci.
  doi: 10.1073/pnas.1719398115
– volume: 475
  start-page: 324
  year: 2011
  end-page: 332
  ident: CR2
  article-title: Molecular chaperones in protein folding and proteostasis
  publication-title: Nature
  doi: 10.1038/nature10317
– volume: 86
  start-page: 1607
  year: 2021
  end-page: 1623
  ident: CR54
  article-title: Mutations in the yeast Cox12 subunit severely compromise the activity of the mitochondrial complex IV
  publication-title: Biochem. Mosc.
  doi: 10.1134/S0006297921120105
– volume: 401
  start-page: 1233
  year: 2020
  end-page: 1248
  ident: CR12
  article-title: Hsp70-mediated quality control: should I stay or should I go?
  publication-title: Biol. Chem.
  doi: 10.1515/hsz-2020-0187
– volume: 5
  start-page: e18638
  year: 2016
  ident: CR73
  article-title: Dynamic control of Hsf1 during heat shock by a chaperone switch and phosphorylation
  publication-title: Elife
  doi: 10.7554/eLife.18638
– volume: 198
  start-page: 387
  year: 2012
  end-page: 404
  ident: CR60
  article-title: Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201201074
– volume: 37
  start-page: e00027
  year: 2017
  end-page: 17
  ident: CR62
  article-title: Coordinated Hsp110 and Hsp104 activities power protein disaggregation in Saccharomyces cerevisiae
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.00027-17
– volume: 182
  start-page: 51
  year: 2021
  end-page: 60
  ident: CR79
  article-title: Purification and characterization of a novel and conserved TPR-domain protein that binds both Hsp90 and Hsp70 and is expressed in all developmental stages of Leishmania major
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2020.12.017
– volume: 9
  start-page: 109
  year: 2004
  end-page: 121
  ident: CR85
  article-title: Tetratricopeptide repeat cochaperones in steroid receptor complexes
  publication-title: Cell Stress Chaperones
  doi: 10.1379/CSC-31.1
– volume: 186
  start-page: 243
  year: 2023
  end-page: 278
  ident: CR11
  article-title: Hallmarks of aging: an expanding universe
  publication-title: Cell
  doi: 10.1016/j.cell.2022.11.001
– volume: 18
  start-page: 623
  year: 2019
  end-page: 632
  ident: CR99
  article-title: Cytoscape stringApp: network analysis and visualization of proteomics data
  publication-title: J. Proteom. Res.
  doi: 10.1021/acs.jproteome.8b00702
– volume: 39
  start-page: 247
  year: 2022
  end-page: 261
  ident: CR18
  article-title: Yeast stress granules at a glance
  publication-title: Yeast
  doi: 10.1002/yea.3681
– volume: 94
  start-page: 73
  year: 1998
  end-page: 82
  ident: CR41
  article-title: Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81223-4
– volume: 16
  start-page: fow027
  year: 2016
  ident: CR93
  article-title: New integrative modules for multicolor-protein labeling and live-cell imaging in Saccharomyces cerevisiae
  publication-title: FEMS Yeast Res.
  doi: 10.1093/femsyr/fow027
– volume: 594
  start-page: 2770
  year: 2020
  end-page: 2781
  ident: CR7
  article-title: Recent advances in understanding catalysis of protein folding by molecular chaperones
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.13844
– volume: 68
  start-page: 87
  year: 2008
  end-page: 97
  ident: CR33
  article-title: Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2008.06135.x
– volume: 248
  start-page: 1112
  year: 1990
  end-page: 1115
  ident: CR43
  article-title: HSP104 required for induced thermotolerance
  publication-title: Science
  doi: 10.1126/science.2188365
– ident: CR69
– volume: 26
  start-page: 668
  year: 2016
  end-page: 679
  ident: CR19
  article-title: Principles and properties of stress granules
  publication-title: Trends Cell Biol.
  doi: 10.1016/j.tcb.2016.05.004
– volume: 9
  year: 2019
  ident: CR82
  article-title: The cochaperone CHIP marks Hsp70- and Hsp90-bound substrates for degradation through a very flexible mechanism
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-019-41060-0
– volume: 20
  start-page: 397
  year: 2012
  end-page: 405
  ident: CR84
  article-title: Structural and functional discussion of the Tetra-Trico-Peptide repeat, a protein interaction module
  publication-title: Structure
  doi: 10.1016/j.str.2012.01.006
– volume: 11
  start-page: 2357
  year: 1992
  end-page: 2364
  ident: CR39
  article-title: Hsp104 is required for tolerance to many forms of stress
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1992.tb05295.x
– volume: 43
  start-page: 7
  year: 2001
  end-page: 10
  ident: CR59
  article-title: Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions
  publication-title: Curr. Microbiol.
  doi: 10.1007/s002840010251
– volume: 216
  start-page: 4027
  year: 2017
  end-page: 4040
  ident: CR65
  article-title: Selective aggregation of the splicing factor Hsh155 suppresses splicing upon genotoxic stress
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201612018
– volume: 51
  start-page: 497
  year: 2016
  end-page: 512
  ident: CR27
  article-title: Proteasome dynamics between proliferation and quiescence stages of Saccharomyces cerevisiae
  publication-title: Crit. Rev. Biochem. Mol. Biol.
  doi: 10.1080/10409238.2016.1230087
– volume: 69
  start-page: 49
  year: 2017
  end-page: 54
  ident: CR71
  article-title: When proteostasis goes bad: protein aggregation in the cell
  publication-title: IUBMB Life
  doi: 10.1002/iub.1597
– volume: 82
  start-page: 555
  year: 2022
  end-page: 569.e7
  ident: CR76
  article-title: NudC guides client transfer between the Hsp40/70 and Hsp90 chaperone systems
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2021.12.031
– volume: 29
  start-page: 22
  year: 2022
  end-page: 36
  ident: CR13
  article-title: Biophysical insight into protein folding, aggregate formation and its inhibition strategies
  publication-title: Protein Pept. Lett
  doi: 10.2174/0929866528666211125114421
– volume: 43
  start-page: 285
  year: 2018
  end-page: 300
  ident: CR29
  article-title: Protein disaggregation in multicellular organisms
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2018.02.003
– volume: 19
  start-page: 2123
  year: 2010
  end-page: 2133
  ident: CR53
  article-title: mip1 containing mutations associated with mitochondrial disease causes mutagenesis and depletion of mtDNA in Saccharomyces cerevisiae
  publication-title: Hum. Mol. Genet.
  doi: 10.1093/hmg/ddq089
– volume: 39
  start-page: 1523
  year: 2001
  end-page: 1532
  ident: CR36
  article-title: Hsf1p and Msn2/4p cooperate in the expression of Saccharomyces cerevisiae genes HSP26 and HSP104 in a gene- and stress type-dependent manner
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2001.02339.x
– volume: 9
  start-page: 1106477
  year: 2022
  ident: CR31
  article-title: Balanced activities of Hsp70 and the ubiquitin proteasome system underlie cellular protein homeostasis
  publication-title: Front. Mol. Biosci.
  doi: 10.3389/fmolb.2022.1106477
– volume: 33
  start-page: 191
  year: 2016
  end-page: 200
  ident: CR100
  article-title: Luciferase NanoLuc as a reporter for gene expression and protein levels in Saccharomyces cerevisiae
  publication-title: Yeast
  doi: 10.1002/yea.3155
– volume: 176
  start-page: 5802
  year: 1994
  end-page: 5813
  ident: CR57
  article-title: Protein synthesis in long-term stationary-phase cultures of Saccharomyces cerevisiae
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.176.18.5802-5813.1994
– volume: 21
  start-page: 947
  year: 2004
  end-page: 962
  ident: CR92
  article-title: A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes
  publication-title: Yeast
  doi: 10.1002/yea.1142
– volume: 43
  start-page: 8107
  year: 2004
  end-page: 8115
  ident: CR42
  article-title: Saccharomyces cerevisiae Hsp104 enhances the chaperone capacity of human cells and inhibits heat stress-induced proapoptotic signaling
  publication-title: Biochemistry
  doi: 10.1021/bi0493766
– volume: 6
  start-page: 1321
  year: 2011
  end-page: 1326
  ident: CR55
  article-title: Caught in the act: covalent crosslinking captures activator-coactivator interactions in vivo
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb200308e
– volume: 148
  start-page: 635
  year: 2000
  end-page: 652
  ident: CR51
  article-title: The yeast nuclear pore complex: composition, architecture, and transport mechanism
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.148.4.635
– volume: 23
  start-page: 2452
  year: 2013
  end-page: 2462
  ident: CR14
  article-title: Coordination of translational control and protein homeostasis during severe heat stress
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2013.09.058
– volume: 10
  start-page: e1001346
  year: 2012
  ident: CR64
  article-title: Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.1001346
– volume: 357
  start-page: 273
  year: 2017
  end-page: 279
  ident: CR40
  article-title: Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104
  publication-title: Science
  doi: 10.1126/science.aan1052
– volume: 20
  start-page: 4618
  year: 2022
  end-page: 4625
  ident: CR46
  article-title: Quality control of cytoplasmic proteins inside the nucleus
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2022.08.033
– volume: 79
  start-page: 1051
  year: 2020
  end-page: 1065.e10
  ident: CR101
  article-title: Molecular connectivity of mitochondrial gene expression and OXPHOS biogenesis
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2020.07.024
– volume: 93
  start-page: 252
  year: 2010
  end-page: 276
  ident: CR86
  article-title: Structure and function of the molecular chaperone Hsp104 from yeast
  publication-title: Biopolymers
  doi: 10.1002/bip.21301
– volume: 21
  start-page: 1406
  year: 2015
  end-page: 1415
  ident: CR9
  article-title: Proteostasis and aging
  publication-title: Nat. Med.
  doi: 10.1038/nm.4001
– volume: 5
  start-page: 2315
  year: 1991
  end-page: 2326
  ident: CR56
  article-title: A general topoisomerase I-dependent transcriptional repression in the stationary phase in yeast
  publication-title: Genes Dev.
  doi: 10.1101/gad.5.12a.2315
– volume: 49
  start-page: 411
  year: 2013
  end-page: 421
  ident: CR70
  article-title: The ribosome as a hub for protein quality control
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2013.01.020
– volume: 38
  start-page: 12
  year: 2021
  end-page: 29
  ident: CR16
  article-title: Cellular quiescence in budding yeast
  publication-title: Yeast
  doi: 10.1002/yea.3545
– volume: 11
  start-page: a034066
  year: 2019
  ident: CR5
  article-title: Tailoring of proteostasis networks with heat shock factors
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a034066
– volume: 63
  start-page: 60
  year: 2016
  end-page: 71
  ident: CR75
  article-title: Defining the essential function of yeast Hsf1 reveals a compact transcriptional program for maintaining eukaryotic proteostasis
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2016.05.014
– volume: 10
  start-page: 1155521
  year: 2023
  ident: CR4
  article-title: Reversible protein assemblies in the proteostasis network in health and disease
  publication-title: Front. Mol. Biosci.
  doi: 10.3389/fmolb.2023.1155521
– volume: 365
  start-page: 342
  year: 2019
  end-page: 347
  ident: CR48
  article-title: The nucleolus functions as a phase-separated protein quality control compartment
  publication-title: Science
  doi: 10.1126/science.aaw9157
– volume: 294
  start-page: 2364
  year: 2001
  end-page: 2368
  ident: CR98
  article-title: Systematic genetic analysis with ordered arrays of yeast deletion mutants
  publication-title: Science
  doi: 10.1126/science.1065810
– volume: 22
  start-page: 3613
  year: 2003
  end-page: 3623
  ident: CR83
  article-title: Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system
  publication-title: EMBO J.
  doi: 10.1093/emboj/cdg362
– volume: 18
  start-page: 754
  year: 1999
  end-page: 762
  ident: CR77
  article-title: Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
  publication-title: EMBO J.
  doi: 10.1093/emboj/18.3.754
– volume: 5
  start-page: 802
  year: 2013
  end-page: 812
  ident: CR72
  article-title: Enhancing protein disaggregation restores proteasome activity in aged cells
  publication-title: Aging
  doi: 10.18632/aging.100613
– volume: 17
  start-page: 1730
  year: 2018
  end-page: 1740
  ident: CR102
  article-title: Extending the compatibility of the SP3 paramagnetic bead processing approach for proteomics
  publication-title: J. Proteom. Res.
  doi: 10.1021/acs.jproteome.7b00913
– volume: 478
  start-page: 3125
  year: 2021
  end-page: 3143
  ident: CR89
  article-title: Quality control of protein import into mitochondria
  publication-title: Biochem. J.
  doi: 10.1042/BCJ20190584
– volume: 117
  start-page: 21804
  year: 2020
  end-page: 21812
  ident: CR66
  article-title: Proteome reallocation from amino acid biosynthesis to ribosomes enables yeast to grow faster in rich media
  publication-title: Proc. Natl Acad. Sci.
  doi: 10.1073/pnas.1921890117
– volume: 76
  start-page: 286
  year: 2019
  end-page: 294
  ident: CR24
  article-title: Properties of stress granule and P-body proteomes
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.09.014
– volume: 34
  start-page: 778
  year: 2015
  end-page: 797
  ident: CR47
  article-title: Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition
  publication-title: EMBO J.
  doi: 10.15252/embj.201489524
– volume: 5
  start-page: e18413
  year: 2016
  ident: CR21
  article-title: Distinct stages in stress granule assembly and disassembly
  publication-title: Elife
  doi: 10.7554/eLife.18413
– volume: 54
  start-page: 7120
  year: 2015
  end-page: 7131
  ident: CR78
  article-title: Specific binding of tetratricopeptide repeat (TPR) proteins to heat shock protein 70 (Hsp70) and heat shock protein 90 (Hsp90) is regulated by affinity and phosphorylation
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b00801
– volume: 36
  start-page: 120
  year: 2008
  end-page: 125
  ident: CR30
  article-title: Common and specific mechanisms of AAA+ proteins involved in protein quality control
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0360120
– volume: 32
  start-page: 1800
  year: 2021
  end-page: 1806
  ident: CR74
  article-title: Hsf1 activation by proteotoxic stress requires concurrent protein synthesis
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.E21-01-0014
– volume: 6
  start-page: 209
  year: 2010
  end-page: 217
  ident: CR58
  article-title: Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.304
– volume: 21
  start-page: 7569
  year: 2001
  end-page: 7575
  ident: CR50
  article-title: Hsp104 interacts with Hsp90 cochaperones in respiring yeast
  publication-title: Mol. Cell Biol
  doi: 10.1128/MCB.21.22.7569-7575.2001
– volume: 18
  start-page: e1700108
  year: 2018
  ident: CR6
  article-title: Protein turnover in aging and longevity
  publication-title: Proteomics
  doi: 10.1002/pmic.201700108
– volume: 20
  start-page: 421
  year: 2019
  end-page: 435
  ident: CR3
  article-title: The proteostasis network and its decline in ageing
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-019-0101-y
– volume: 11
  start-page: 777
  year: 2010
  end-page: 788
  ident: CR1
  article-title: Cellular strategies for controlling protein aggregation
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm2993
– ident: CR23
– volume: 60
  start-page: 2349
  year: 2021
  end-page: 2363
  ident: CR81
  article-title: Optimizing the first TPR domain of the human SPAG1 protein provides insight into the HSP70 and HSP90 binding properties
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.1c00052
– volume: 22
  start-page: 3127
  year: 2011
  end-page: 3138
  ident: CR38
  article-title: Fine-tuning of the Msn2/4-mediated yeast stress responses as revealed by systematic deletion of Msn2/4 partners
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e10-12-1007
– volume: 31
  start-page: 107680
  year: 2020
  ident: CR63
  article-title: Chaperone-mediated protein disaggregation triggers proteolytic clearance of intra-nuclear protein inclusions
  publication-title: Cell. Rep.
  doi: 10.1016/j.celrep.2020.107680
– volume: 32
  start-page: D311
  year: 2004
  end-page: D314
  ident: CR104
  article-title: Saccharomyces Genome Database (SGD) provides tools to identify and analyze sequences from Saccharomyces cerevisiae and related sequences from other organisms
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkh033
– volume: 14
  start-page: 2394
  year: 2015
  end-page: 2404
  ident: CR103
  article-title: A scalable approach for protein false discovery rate estimation in large proteomic data sets
  publication-title: Mol. Cell Proteom.
  doi: 10.1074/mcp.M114.046995
– volume: 129
  start-page: 1190
  year: 2016
  end-page: 1197
  ident: CR26
  article-title: Proteasome storage granules are transiently associated with the insoluble protein deposit in Saccharomyces cerevisiae
  publication-title: J. Cell Sci.
– volume: 126
  start-page: 12
  year: 2017
  end-page: 17
  ident: CR20
  article-title: Isolation of yeast and mammalian stress granule cores
  publication-title: Methods
  doi: 10.1016/j.ymeth.2017.04.020
– volume: 298
  start-page: 102199
  year: 2022
  ident: CR44
  article-title: Nuclear protein quality control in yeast: the latest INQuiries
  publication-title: J. Biol. Chem.
  doi: 10.1016/j.jbc.2022.102199
– volume: 1233
  start-page: 101
  year: 2020
  end-page: 115
  ident: CR10
  article-title: Proteostasis dysregulation in pancreatic cancer
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-3-030-38266-7_4
– volume: 44
  start-page: 21
  year: 2002
  end-page: 35
  ident: CR37
  article-title: HSF and Msn2/4p can exclusively or cooperatively activate the yeast HSP104 gene
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2002.02860.x
– volume: 70
  start-page: 603
  year: 2001
  end-page: 647
  ident: CR67
  article-title: Folding of newly translated proteins in vivo: the role of molecular chaperones
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.70.1.603
– volume: 146
  start-page: 90
  year: 2004
  end-page: 98
  ident: CR32
  article-title: Broad yet high substrate specificity: the challenge of AAA+ proteins
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2003.10.009
– volume: 116
  start-page: 71
  year: 1996
  end-page: 76
  ident: CR96
  article-title: Computer visualization of three-dimensional image data using IMOD
  publication-title: J. Struct. Biol.
  doi: 10.1006/jsbi.1996.0013
– volume: 2
  start-page: 31
  year: 2007
  end-page: 34
  ident: CR91
  article-title: High-efficiency yeast transformation using the LiAc/SS carrier DNA/PEG method
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2007.13
– volume: 11
  start-page: a034033
  year: 2019
  ident: CR35
  article-title: Spiraling in control: structures and mechanisms of the Hsp104 disaggregase
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a034033
– volume: 34
  start-page: 108637
  year: 2021
  ident: CR95
  article-title: Snd3 controls nucleus-vacuole junctions in response to glucose signaling
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2020.108637
– volume: 21
  start-page: 932
  year: 1999
  end-page: 939
  ident: CR87
  article-title: The tetratricopeptide repeat: a structural motif mediating protein-protein interactions
  publication-title: BioEssays
  doi: 10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N
– volume: 132
  start-page: jcs213025
  year: 2019
  ident: CR17
  article-title: The cell biology of quiescent yeast – a diversity of individual scenarios
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.213025
– volume: 18
  start-page: 210
  year: 2011
  end-page: 221
  ident: CR61
  article-title: Chemical screens against a reconstituted multi-protein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism
  publication-title: Chem. Biol.
  doi: 10.1016/j.chembiol.2010.12.010
– volume: 176
  start-page: 5802
  year: 1994
  ident: 44538_CR57
  publication-title: J. Bacteriol.
  doi: 10.1128/jb.176.18.5802-5813.1994
– volume: 186
  start-page: 243
  year: 2023
  ident: 44538_CR11
  publication-title: Cell
  doi: 10.1016/j.cell.2022.11.001
– volume: 21
  start-page: 932
  year: 1999
  ident: 44538_CR87
  publication-title: BioEssays
  doi: 10.1002/(SICI)1521-1878(199911)21:11<932::AID-BIES5>3.0.CO;2-N
– volume: 23
  start-page: 2452
  year: 2013
  ident: 44538_CR14
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2013.09.058
– volume: 19
  start-page: 2123
  year: 2010
  ident: 44538_CR53
  publication-title: Hum. Mol. Genet.
  doi: 10.1093/hmg/ddq089
– volume: 132
  start-page: jcs213025
  year: 2019
  ident: 44538_CR17
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.213025
– volume: 82
  start-page: 555
  year: 2022
  ident: 44538_CR76
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2021.12.031
– volume: 18
  start-page: 623
  year: 2019
  ident: 44538_CR99
  publication-title: J. Proteom. Res.
  doi: 10.1021/acs.jproteome.8b00702
– volume: 10
  start-page: e1001346
  year: 2012
  ident: 44538_CR64
  publication-title: PLoS Biol.
  doi: 10.1371/journal.pbio.1001346
– volume: 60
  start-page: 2349
  year: 2021
  ident: 44538_CR81
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.1c00052
– volume: 431
  start-page: 2180
  year: 2019
  ident: 44538_CR34
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2019.04.014
– volume: 117
  start-page: 1485
  year: 2020
  ident: 44538_CR68
  publication-title: Proc. Natl Acad. Sci.
  doi: 10.1073/pnas.1913207117
– volume: 20
  start-page: 421
  year: 2019
  ident: 44538_CR3
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/s41580-019-0101-y
– volume: 22
  start-page: 3613
  year: 2003
  ident: 44538_CR83
  publication-title: EMBO J.
  doi: 10.1093/emboj/cdg362
– ident: 44538_CR22
  doi: 10.15252/embj.2022111802
– ident: 44538_CR23
  doi: 10.7554/eLife.56525
– volume: 248
  start-page: 1112
  year: 1990
  ident: 44538_CR43
  publication-title: Science
  doi: 10.1126/science.2188365
– volume: 5
  start-page: e18638
  year: 2016
  ident: 44538_CR73
  publication-title: Elife
  doi: 10.7554/eLife.18638
– volume: 32
  start-page: 1800
  year: 2021
  ident: 44538_CR74
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.E21-01-0014
– volume: 126
  start-page: 12
  year: 2017
  ident: 44538_CR20
  publication-title: Methods
  doi: 10.1016/j.ymeth.2017.04.020
– volume: 10
  start-page: e65484
  year: 2021
  ident: 44538_CR90
  publication-title: eLife
  doi: 10.7554/eLife.65484
– volume: 21
  start-page: 947
  year: 2004
  ident: 44538_CR92
  publication-title: Yeast
  doi: 10.1002/yea.1142
– volume: 32
  start-page: D311
  year: 2004
  ident: 44538_CR104
  publication-title: Nuc. Acids Res.
  doi: 10.1093/nar/gkh033
– ident: 44538_CR69
  doi: 10.1016/j.mcpro.2023.100552
– volume: 36
  start-page: 120
  year: 2008
  ident: 44538_CR30
  publication-title: Biochem. Soc. Trans.
  doi: 10.1042/BST0360120
– volume: 17
  start-page: 1730
  year: 2018
  ident: 44538_CR102
  publication-title: J. Proteom. Res.
  doi: 10.1021/acs.jproteome.7b00913
– volume: 353
  start-page: aac4354
  year: 2016
  ident: 44538_CR8
  publication-title: Science
  doi: 10.1126/science.aac4354
– volume: 115
  start-page: E3969
  year: 2018
  ident: 44538_CR52
  publication-title: Proc. Natl Acad. Sci.
  doi: 10.1073/pnas.1719398115
– volume: 101
  start-page: 199
  year: 2000
  ident: 44538_CR80
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)80830-2
– volume: 2
  start-page: 31
  year: 2007
  ident: 44538_CR91
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2007.13
– volume: 14
  start-page: 2394
  year: 2015
  ident: 44538_CR103
  publication-title: Mol. Cell Proteom.
  doi: 10.1074/mcp.M114.046995
– volume: 216
  start-page: 4027
  year: 2017
  ident: 44538_CR65
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201612018
– volume: 20
  start-page: 4618
  year: 2022
  ident: 44538_CR46
  publication-title: Comput. Struct. Biotechnol. J.
  doi: 10.1016/j.csbj.2022.08.033
– volume: 37
  start-page: e00027
  year: 2017
  ident: 44538_CR62
  publication-title: Mol. Cell. Biol.
  doi: 10.1128/MCB.00027-17
– ident: 44538_CR45
  doi: 10.1038/s41556-023-01128-6
– volume: 69
  start-page: 214
  year: 2018
  ident: 44538_CR28
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2018.01.004
– volume: 425
  start-page: 686
  year: 2003
  ident: 44538_CR49
  publication-title: Nature
  doi: 10.1038/nature02026
– volume: 39
  start-page: 247
  year: 2022
  ident: 44538_CR18
  publication-title: Yeast
  doi: 10.1002/yea.3681
– volume: 146
  start-page: 90
  year: 2004
  ident: 44538_CR32
  publication-title: J. Struct. Biol.
  doi: 10.1016/j.jsb.2003.10.009
– volume: 365
  start-page: 342
  year: 2019
  ident: 44538_CR48
  publication-title: Science
  doi: 10.1126/science.aaw9157
– volume: 294
  start-page: 2364
  year: 2001
  ident: 44538_CR98
  publication-title: Science
  doi: 10.1126/science.1065810
– volume: 21
  start-page: 1406
  year: 2015
  ident: 44538_CR9
  publication-title: Nat. Med.
  doi: 10.1038/nm.4001
– volume: 31
  start-page: 107680
  year: 2020
  ident: 44538_CR63
  publication-title: Cell. Rep.
  doi: 10.1016/j.celrep.2020.107680
– volume: 43
  start-page: 285
  year: 2018
  ident: 44538_CR29
  publication-title: Trends Biochem. Sci.
  doi: 10.1016/j.tibs.2018.02.003
– volume: 5
  start-page: 802
  year: 2013
  ident: 44538_CR72
  publication-title: Aging
  doi: 10.18632/aging.100613
– volume: 6
  start-page: 1321
  year: 2011
  ident: 44538_CR55
  publication-title: ACS Chem. Biol.
  doi: 10.1021/cb200308e
– volume: 63
  start-page: 60
  year: 2016
  ident: 44538_CR75
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2016.05.014
– volume: 129
  start-page: 1190
  year: 2016
  ident: 44538_CR26
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.179648
– volume: 9
  start-page: 1106477
  year: 2022
  ident: 44538_CR31
  publication-title: Front. Mol. Biosci.
  doi: 10.3389/fmolb.2022.1106477
– volume: 33
  start-page: 191
  year: 2016
  ident: 44538_CR100
  publication-title: Yeast
  doi: 10.1002/yea.3155
– volume: 6
  start-page: 209
  year: 2010
  ident: 44538_CR58
  publication-title: Nat. Chem. Biol.
  doi: 10.1038/nchembio.304
– volume: 18
  start-page: e1700108
  year: 2018
  ident: 44538_CR6
  publication-title: Proteomics
  doi: 10.1002/pmic.201700108
– volume: 20
  start-page: 397
  year: 2012
  ident: 44538_CR84
  publication-title: Structure
  doi: 10.1016/j.str.2012.01.006
– volume: 9
  start-page: 109
  year: 2004
  ident: 44538_CR85
  publication-title: Cell Stress Chaperones
  doi: 10.1379/CSC-31.1
– volume: 11
  start-page: 2357
  year: 1992
  ident: 44538_CR39
  publication-title: EMBO J.
  doi: 10.1002/j.1460-2075.1992.tb05295.x
– volume: 54
  start-page: 43
  year: 2019
  ident: 44538_CR88
  publication-title: Current Opin. Struct. Biol.
  doi: 10.1016/j.sbi.2018.12.004
– volume: 401
  start-page: 1233
  year: 2020
  ident: 44538_CR12
  publication-title: Biol. Chem.
  doi: 10.1515/hsz-2020-0187
– volume: 5
  start-page: 2315
  year: 1991
  ident: 44538_CR56
  publication-title: Genes Dev.
  doi: 10.1101/gad.5.12a.2315
– volume: 34
  start-page: 778
  year: 2015
  ident: 44538_CR47
  publication-title: EMBO J.
  doi: 10.15252/embj.201489524
– volume: 51
  start-page: 497
  year: 2016
  ident: 44538_CR27
  publication-title: Crit. Rev. Biochem. Mol. Biol.
  doi: 10.1080/10409238.2016.1230087
– volume: 116
  start-page: 71
  year: 1996
  ident: 44538_CR96
  publication-title: J. Struct. Biol.
  doi: 10.1006/jsbi.1996.0013
– volume: 148
  start-page: 635
  year: 2000
  ident: 44538_CR51
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.148.4.635
– volume: 1233
  start-page: 101
  year: 2020
  ident: 44538_CR10
  publication-title: Adv. Exp. Med. Biol.
  doi: 10.1007/978-3-030-38266-7_4
– volume: 18
  start-page: 210
  year: 2011
  ident: 44538_CR61
  publication-title: Chem. Biol.
  doi: 10.1016/j.chembiol.2010.12.010
– volume: 18
  start-page: 754
  year: 1999
  ident: 44538_CR77
  publication-title: EMBO J.
  doi: 10.1093/emboj/18.3.754
– volume: 594
  start-page: 2770
  year: 2020
  ident: 44538_CR7
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.13844
– volume: 303
  start-page: 808
  year: 2004
  ident: 44538_CR97
  publication-title: Science
  doi: 10.1126/science.1091317
– volume: 117
  start-page: 21804
  year: 2020
  ident: 44538_CR66
  publication-title: Proc. Natl Acad. Sci.
  doi: 10.1073/pnas.1921890117
– volume: 9
  year: 2019
  ident: 44538_CR82
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-019-41060-0
– volume: 11
  start-page: 777
  year: 2010
  ident: 44538_CR1
  publication-title: Nat. Rev. Mol. Cell Biol.
  doi: 10.1038/nrm2993
– volume: 22
  start-page: 3127
  year: 2011
  ident: 44538_CR38
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e10-12-1007
– volume: 26
  start-page: 668
  year: 2016
  ident: 44538_CR19
  publication-title: Trends Cell Biol.
  doi: 10.1016/j.tcb.2016.05.004
– volume: 198
  start-page: 387
  year: 2012
  ident: 44538_CR60
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201201074
– volume: 21
  start-page: 7569
  year: 2001
  ident: 44538_CR50
  publication-title: Mol. Cell Biol
  doi: 10.1128/MCB.21.22.7569-7575.2001
– volume: 94
  start-page: 73
  year: 1998
  ident: 44538_CR41
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81223-4
– volume: 475
  start-page: 324
  year: 2011
  ident: 44538_CR2
  publication-title: Nature
  doi: 10.1038/nature10317
– volume: 86
  start-page: 1607
  year: 2021
  ident: 44538_CR54
  publication-title: Biochem. Mosc.
  doi: 10.1134/S0006297921120105
– volume: 29
  start-page: 22
  year: 2022
  ident: 44538_CR13
  publication-title: Protein Pept. Lett
  doi: 10.2174/0929866528666211125114421
– volume: 68
  start-page: 87
  year: 2008
  ident: 44538_CR33
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2008.06135.x
– volume: 5
  start-page: e18413
  year: 2016
  ident: 44538_CR21
  publication-title: Elife
  doi: 10.7554/eLife.18413
– volume: 79
  start-page: 1051
  year: 2020
  ident: 44538_CR101
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2020.07.024
– volume: 39
  start-page: 1523
  year: 2001
  ident: 44538_CR36
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2001.02339.x
– volume: 93
  start-page: 252
  year: 2010
  ident: 44538_CR86
  publication-title: Biopolymers
  doi: 10.1002/bip.21301
– volume: 298
  start-page: 102199
  year: 2022
  ident: 44538_CR44
  publication-title: J. Biol. Chem.
  doi: 10.1016/j.jbc.2022.102199
– volume: 10
  start-page: 1155521
  year: 2023
  ident: 44538_CR4
  publication-title: Front. Mol. Biosci.
  doi: 10.3389/fmolb.2023.1155521
– volume: 334
  start-page: 1074
  year: 2011
  ident: 44538_CR15
  publication-title: Science
  doi: 10.1126/science.1216242
– volume: 76
  start-page: 286
  year: 2019
  ident: 44538_CR24
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2019.09.014
– volume: 44
  start-page: 21
  year: 2002
  ident: 44538_CR37
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2002.02860.x
– volume: 478
  start-page: 3125
  year: 2021
  ident: 44538_CR89
  publication-title: Biochem. J.
  doi: 10.1042/BCJ20190584
– volume: 69
  start-page: 49
  year: 2017
  ident: 44538_CR71
  publication-title: IUBMB Life
  doi: 10.1002/iub.1597
– volume: 7
  start-page: e34532
  year: 2018
  ident: 44538_CR25
  publication-title: eLife
  doi: 10.7554/eLife.34532
– volume: 49
  start-page: 411
  year: 2013
  ident: 44538_CR70
  publication-title: Mol. Cell
  doi: 10.1016/j.molcel.2013.01.020
– volume: 70
  start-page: 603
  year: 2001
  ident: 44538_CR67
  publication-title: Annu. Rev. Biochem.
  doi: 10.1146/annurev.biochem.70.1.603
– volume: 54
  start-page: 7120
  year: 2015
  ident: 44538_CR78
  publication-title: Biochemistry
  doi: 10.1021/acs.biochem.5b00801
– volume: 11
  start-page: a034033
  year: 2019
  ident: 44538_CR35
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a034033
– volume: 38
  start-page: 12
  year: 2021
  ident: 44538_CR16
  publication-title: Yeast
  doi: 10.1002/yea.3545
– volume: 9
  start-page: 676
  year: 2012
  ident: 44538_CR94
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.2019
– volume: 43
  start-page: 7
  year: 2001
  ident: 44538_CR59
  publication-title: Curr. Microbiol.
  doi: 10.1007/s002840010251
– volume: 16
  start-page: fow027
  year: 2016
  ident: 44538_CR93
  publication-title: FEMS Yeast Res.
  doi: 10.1093/femsyr/fow027
– volume: 182
  start-page: 51
  year: 2021
  ident: 44538_CR79
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2020.12.017
– volume: 11
  start-page: a034066
  year: 2019
  ident: 44538_CR5
  publication-title: Cold Spring Harb. Perspect. Biol.
  doi: 10.1101/cshperspect.a034066
– volume: 43
  start-page: 8107
  year: 2004
  ident: 44538_CR42
  publication-title: Biochemistry
  doi: 10.1021/bi0493766
– volume: 357
  start-page: 273
  year: 2017
  ident: 44538_CR40
  publication-title: Science
  doi: 10.1126/science.aan1052
– volume: 34
  start-page: 108637
  year: 2021
  ident: 44538_CR95
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2020.108637
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Snippet The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a key quality...
Abstract The resilience of cellular proteostasis declines with age, which drives protein aggregation and compromises viability. The nucleus has emerged as a...
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Heat-Shock Proteins - metabolism
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Title Nuclear Hsp104 safeguards the dormant translation machinery during quiescence
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