Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy

The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation, and a translational stress response that includes st...

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Published inMolecular cell Vol. 81; no. 20; pp. 4209 - 4227.e12
Main Authors Jiang, Lulu, Lin, Weiwei, Zhang, Cheng, Ash, Peter E.A., Verma, Mamta, Kwan, Julian, van Vliet, Emily, Yang, Zhuo, Cruz, Anna Lourdes, Boudeau, Samantha, Maziuk, Brandon F., Lei, Shuwen, Song, Jaehyup, Alvarez, Victor E., Hovde, Stacy, Abisambra, Jose F., Kuo, Min-Hao, Kanaan, Nicholas, Murray, Melissa E., Crary, John F., Zhao, Jian, Cheng, Ji-Xin, Petrucelli, Leonard, Li, Hu, Emili, Andrew, Wolozin, Benjamin
Format Journal Article
LanguageEnglish
Published Elsevier Inc 21.10.2021
Subjects
Online AccessGet full text
ISSN1097-2765
1097-4164
1097-4164
DOI10.1016/j.molcel.2021.07.038

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Abstract The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation, and a translational stress response that includes stress granules and reduced protein synthesis. Proteomic analysis identifies HNRNPA2B1 as a principle target of oTau-c. The association of HNRNPA2B1 with endogenous oTau was verified in neurons, animal models, and human Alzheimer brain tissues. Mechanistic studies demonstrate that HNRNPA2B1 functions as a linker, connecting oTau with N6-methyladenosine (m6A) modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau or oTau-c from associating with m6A or from reducing protein synthesis and reduces oTau-induced neurodegeneration. Levels of m6A and the m6A-oTau-HNRNPA2B1 complex are increased up to 5-fold in the brains of Alzheimer subjects and P301S tau mice. These results reveal a complex containing oTau, HNRNPA2B1, and m6A that contributes to the integrated stress response of oTau. [Display omitted] •Tau oligomerization exhibits rapid aggregation of proteins linked to RNA metabolism•Oligomeric tau complexes with HNRNPA2B1 and m6A-RNA to regulate RNA translation•Knockdown of HNRNPA2B1 reduces the response to pathological tau•m6A progressively increases with disease severity in human AD brains Oligomerization of microtubule-associated protein tau recruits RNA binding proteins and methylated RNA transcripts, termed N6-methyladenosine RNA. This complex regulates the stress response and inhibits protein synthesis. In Alzheimer’s disease and related models, this complex becomes persistent and pathological, leading to tau fibrillization, nuclear membrane disruption, and progressive neurodegeneration.
AbstractList The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation, and a translational stress response that includes stress granules and reduced protein synthesis. Proteomic analysis identifies HNRNPA2B1 as a principle target of oTau-c. The association of HNRNPA2B1 with endogenous oTau was verified in neurons, animal models, and human Alzheimer brain tissues. Mechanistic studies demonstrate that HNRNPA2B1 functions as a linker, connecting oTau with N6-methyladenosine (m6A) modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau or oTau-c from associating with m6A or from reducing protein synthesis and reduces oTau-induced neurodegeneration. Levels of m6A and the m6A-oTau-HNRNPA2B1 complex are increased up to 5-fold in the brains of Alzheimer subjects and P301S tau mice. These results reveal a complex containing oTau, HNRNPA2B1, and m6A that contributes to the integrated stress response of oTau.The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation, and a translational stress response that includes stress granules and reduced protein synthesis. Proteomic analysis identifies HNRNPA2B1 as a principle target of oTau-c. The association of HNRNPA2B1 with endogenous oTau was verified in neurons, animal models, and human Alzheimer brain tissues. Mechanistic studies demonstrate that HNRNPA2B1 functions as a linker, connecting oTau with N6-methyladenosine (m6A) modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau or oTau-c from associating with m6A or from reducing protein synthesis and reduces oTau-induced neurodegeneration. Levels of m6A and the m6A-oTau-HNRNPA2B1 complex are increased up to 5-fold in the brains of Alzheimer subjects and P301S tau mice. These results reveal a complex containing oTau, HNRNPA2B1, and m6A that contributes to the integrated stress response of oTau.
The microtubule associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation and a translational stress response that includes stress granules and reduced protein synthesis. Proteomic analysis identifies HNRNPA2B1 as a principle target of oTau-c. The association of HNRNPA2B1 with endogenous oTau was verified in neurons, animal models and human Alzheimer brain tissues. Mechanistic studies demonstrate that HNRNPA2B1 functions as a linker, connecting oTau with N6-methyladenosine (m6A) modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau or oTau-c from associating with m6A or from reducing protein synthesis, and reduces oTau-induced neurodegeneration. Levels of m6A and the m6A-oTau-HNRNPA2B1 complex are increased up to 5-fold in brains of Alzheimer subjects and P301S tau mice. These results reveal a complex containing oTau, HNRNPA2B1 and m6A that contributes to the integrated stress response of oTau. Oligomerization of microtubule-associated protein tau recruits RNA binding proteins and methylated RNA transcripts, termed N6-methyladenosine RNA. This complex regulates the stress response and inhibits protein synthesis. In Alzheimer’s disease and related models, this complex becomes persistent and pathological, leading to tau fibrillization, nuclear membrane disruption and progressive neurodegeneration.
The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation, and a translational stress response that includes stress granules and reduced protein synthesis. Proteomic analysis identifies HNRNPA2B1 as a principle target of oTau-c. The association of HNRNPA2B1 with endogenous oTau was verified in neurons, animal models, and human Alzheimer brain tissues. Mechanistic studies demonstrate that HNRNPA2B1 functions as a linker, connecting oTau with N⁶-methyladenosine (m⁶A) modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau or oTau-c from associating with m⁶A or from reducing protein synthesis and reduces oTau-induced neurodegeneration. Levels of m⁶A and the m⁶A-oTau-HNRNPA2B1 complex are increased up to 5-fold in the brains of Alzheimer subjects and P301S tau mice. These results reveal a complex containing oTau, HNRNPA2B1, and m⁶A that contributes to the integrated stress response of oTau.
The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau oligomers (oTau-c). Optical induction of oTau-c elicits tau phosphorylation, aggregation, and a translational stress response that includes stress granules and reduced protein synthesis. Proteomic analysis identifies HNRNPA2B1 as a principle target of oTau-c. The association of HNRNPA2B1 with endogenous oTau was verified in neurons, animal models, and human Alzheimer brain tissues. Mechanistic studies demonstrate that HNRNPA2B1 functions as a linker, connecting oTau with N6-methyladenosine (m6A) modified RNA transcripts. Knockdown of HNRNPA2B1 prevents oTau or oTau-c from associating with m6A or from reducing protein synthesis and reduces oTau-induced neurodegeneration. Levels of m6A and the m6A-oTau-HNRNPA2B1 complex are increased up to 5-fold in the brains of Alzheimer subjects and P301S tau mice. These results reveal a complex containing oTau, HNRNPA2B1, and m6A that contributes to the integrated stress response of oTau. [Display omitted] •Tau oligomerization exhibits rapid aggregation of proteins linked to RNA metabolism•Oligomeric tau complexes with HNRNPA2B1 and m6A-RNA to regulate RNA translation•Knockdown of HNRNPA2B1 reduces the response to pathological tau•m6A progressively increases with disease severity in human AD brains Oligomerization of microtubule-associated protein tau recruits RNA binding proteins and methylated RNA transcripts, termed N6-methyladenosine RNA. This complex regulates the stress response and inhibits protein synthesis. In Alzheimer’s disease and related models, this complex becomes persistent and pathological, leading to tau fibrillization, nuclear membrane disruption, and progressive neurodegeneration.
Author Kuo, Min-Hao
Zhao, Jian
Zhang, Cheng
Jiang, Lulu
Alvarez, Victor E.
Verma, Mamta
Hovde, Stacy
Lei, Shuwen
Cheng, Ji-Xin
Song, Jaehyup
van Vliet, Emily
Yang, Zhuo
Cruz, Anna Lourdes
Boudeau, Samantha
Kanaan, Nicholas
Emili, Andrew
Petrucelli, Leonard
Li, Hu
Maziuk, Brandon F.
Murray, Melissa E.
Lin, Weiwei
Wolozin, Benjamin
Ash, Peter E.A.
Kwan, Julian
Abisambra, Jose F.
Crary, John F.
AuthorAffiliation 4 Department of Neurology, Boston University School of Medicine, Boston, MA 02118
6 Department of Neuroscience, University of Florida, Gainesville, FL 32611
11 Center for Neurophotonics, Boston University, Boston, MA 02215
2 Center for Network Systems Biology, Boston University School of Medicine, Boston, MA, 02118
5 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824
3 Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Rochester, MN 55905
9 Department of Pathology, Mount Sinai Medical Center, New York, NY 10029
10 Department of Electrical and Computer Engineering, Boston University, Boston, MA 02459
12 Center for Systems Neuroscience, Boston University, Boston, MA 02215
1 Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118
8 Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224
7 Department of Translational Science and Molecular Medicine, College o
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ContentType Journal Article
Copyright 2021 Elsevier Inc.
Copyright © 2021 Elsevier Inc. All rights reserved.
Copyright_xml – notice: 2021 Elsevier Inc.
– notice: Copyright © 2021 Elsevier Inc. All rights reserved.
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Keywords lamin
tau oligomerization
METTL3
stress granules
nuclear envelope
RNA translation
neurodegeneration
Alzheimer's disease
RNA methylation
fibrils
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AUTHOR CONTRIBUTIONS
Conceptualization: B.W. and L.J.; Methodology: L.J., W.L., P.E.A., C.Z., J.K., M.V., S.B., B.F.M., S.L., A.L.C., J.F.A., E.V.V.; Investigation: L.J., W.L., M.V., P.E.A., E.V.V.; Reagents: L.P., N.K., M.M., J.C., V.E.A, S.H., M.H.K. Visualization: L.J., C.Z., H.L., W.L., J.S., J.Z., J.X.C.; Writing: L.J., B.W.; Editing: B.W., L.J., A.E., W.L., L.P., N.K., P.E.A.; Supervision: B.W., A.E.; Funding Acquisition: B.W, A.E.
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/8541906
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Snippet The microtubule-associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau...
The microtubule associated protein tau oligomerizes, but the actions of oligomeric tau (oTau) are unknown. We have used Cry2-based optogenetics to induce tau...
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SubjectTerms Alzheimer's disease
brain
fibrils
humans
lamin
METTL3
neurodegeneration
neurodegenerative diseases
nuclear envelope
optogenetics
phosphorylation
protein synthesis
proteomics
RNA methylation
RNA translation
stress granules
stress response
tau oligomerization
Title Interaction of tau with HNRNPA2B1 and N6-methyladenosine RNA mediates the progression of tauopathy
URI https://dx.doi.org/10.1016/j.molcel.2021.07.038
https://www.proquest.com/docview/2566030858
https://www.proquest.com/docview/2636846448
https://pubmed.ncbi.nlm.nih.gov/PMC8541906
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