C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins
Zhang et al . show that the poly(GA) proteins produced in patients with C9ORF72 repeat expansions cause neurodegeneration and behavioral abnormalities when expressed in mice. The emergence of these phenotypes requires poly(GA) aggregation, and poly(GA) inclusions sequester HR23 proteins involved in...
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| Published in | Nature neuroscience Vol. 19; no. 5; pp. 668 - 677 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
New York
Nature Publishing Group US
01.05.2016
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 1097-6256 1546-1726 1546-1726 |
| DOI | 10.1038/nn.4272 |
Cover
| Abstract | Zhang
et al
. show that the poly(GA) proteins produced in patients with
C9ORF72
repeat expansions cause neurodegeneration and behavioral abnormalities when expressed in mice. The emergence of these phenotypes requires poly(GA) aggregation, and poly(GA) inclusions sequester HR23 proteins involved in proteasomal degradation, as well as proteins involved in nucleocytoplasmic transport.
Neuronal inclusions of poly(GA), a protein unconventionally translated from G
4
C
2
repeat expansions in
C9ORF72
, are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in
C9ORF72
expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. |
|---|---|
| AbstractList | Neuronal inclusions of poly(GA), a protein unconventionally translated from G4 C2 repeat expansions in C9ORF72, are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. Zhang et al . show that the poly(GA) proteins produced in patients with C9ORF72 repeat expansions cause neurodegeneration and behavioral abnormalities when expressed in mice. The emergence of these phenotypes requires poly(GA) aggregation, and poly(GA) inclusions sequester HR23 proteins involved in proteasomal degradation, as well as proteins involved in nucleocytoplasmic transport. Neuronal inclusions of poly(GA), a protein unconventionally translated from G 4 C 2 repeat expansions in C9ORF72 , are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. Neuronal inclusions of poly(GA), a protein unconventionally translated from G4C2 repeat expansions in C9ORF72, are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology.Neuronal inclusions of poly(GA), a protein unconventionally translated from G4C2 repeat expansions in C9ORF72, are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. Neuronal inclusions of poly(GA), a protein unconventionally translated from G4C2 repeat expansions in C9ORF72, are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. Neuronal inclusions of poly(GA), a protein unconventionally translated from [G.sub.4][C.sub.2] repeat expansions in C9ORF72, are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. Neuronal inclusions of poly(GA), a protein unconventionally translated from G 4 C 2 repeat expansions in C9ORF72 , are abundant in patients with frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) caused by this mutation. To investigate poly(GA) toxicity, we generated mice that exhibit poly(GA) pathology, neurodegeneration and behavioral abnormalities reminiscent of FTD and ALS. These phenotypes occurred in the absence of TDP-43 pathology and required poly(GA) aggregation. HR23 proteins involved in proteasomal degradation and proteins involved in nucleocytoplasmic transport were sequestered by poly(GA) in these mice. HR23A and HR23B similarly colocalized to poly(GA) inclusions in C9ORF72 expansion carriers. Sequestration was accompanied by an accumulation of ubiquitinated proteins and decreased xeroderma pigmentosum C (XPC) levels in mice, indicative of HR23A and HR23B dysfunction. Restoring HR23B levels attenuated poly(GA) aggregation and rescued poly(GA)-induced toxicity in neuronal cultures. These data demonstrate that sequestration and impairment of nuclear HR23 and nucleocytoplasmic transport proteins is an outcome of, and a contributor to, poly(GA) pathology. |
| Audience | Academic |
| Author | Rademakers, Rosa Gendron, Tania F Lin, Wen-Lang Murray, Melissa E Dickey, Chad A Perkerson, Emilie A Wang, Zizhao S Bu, Guojun Cleveland, Don W Stankowski, Jeannette N Xu, Ya-Fei Chew, Jeannie Baker, Jeremy D Sasaguri, Hiroki Tong, Jimei Yue, Mei Kurti, Aishe Grima, Jonathan C Edbauer, Dieter Liesinger, Amanda M Lagier-Tourenne, Clotilde Katzman, Rebecca B Petrucelli, Leonard Zhang, Yong-Jie Gass, Jennifer Link, Christopher D Shinohara, Mitsuru Fryer, John D Garrett, Aliesha Boylan, Kevin B Dickson, Dennis W Rothstein, Jeffrey D Jansen-West, Karen Daughrity, Lillian Castanedes-Casey, Monica Jiang, Jie |
| AuthorAffiliation | 1 Department of Neuroscience, Mayo Clinic, Jacksonville, Florida, USA 3 Brain Science Institute, School of Medicine, Johns Hopkins University, Maryland, USA 12 Department of Cellular and Molecular Medicine, University of California at San Diego, La Jolla, California, USA 2 Department of Neurology, School of Medicine, Johns Hopkins University, Maryland, USA 4 Department of Neuroscience, School of Medicine, Johns Hopkins University, Maryland, USA 11 Munich Cluster of Systems Neurology (SyNergy), Munich, Germany 6 Department of Molecular Medicine, College of Medicine, Byrd Alzheimer’s Institute, University of South Florida, Tampa, Florida, USA 9 German Center for Neurodegenerative Diseases (DZNE), Munich, Germany 13 Department of Neurology, Mayo Clinic, Jacksonville, Florida, USA 10 Institute for Metabolic Biochemistry, Ludwig Maximilians University Munich, Munich, Germany 14 Integrative Physiology, Institute for Behavioral Genetics, University of Colorado, Boulder, Colorado, USA 5 Neurobiology of D |
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| Author_xml | – sequence: 1 givenname: Yong-Jie surname: Zhang fullname: Zhang, Yong-Jie organization: Department of Neuroscience, Mayo Clinic – sequence: 2 givenname: Tania F surname: Gendron fullname: Gendron, Tania F organization: Department of Neuroscience, Mayo Clinic – sequence: 3 givenname: Jonathan C surname: Grima fullname: Grima, Jonathan C organization: Department of Neurology, School of Medicine, Johns Hopkins University, Brain Science Institute, School of Medicine, Johns Hopkins University, Department of Neuroscience, School of Medicine, Johns Hopkins University – sequence: 4 givenname: Hiroki surname: Sasaguri fullname: Sasaguri, Hiroki organization: Department of Neuroscience, Mayo Clinic – sequence: 5 givenname: Karen surname: Jansen-West fullname: Jansen-West, Karen organization: Department of Neuroscience, Mayo Clinic – sequence: 6 givenname: Ya-Fei surname: Xu fullname: Xu, Ya-Fei organization: Department of Neuroscience, Mayo Clinic – sequence: 7 givenname: Rebecca B surname: Katzman fullname: Katzman, Rebecca B organization: Department of Neuroscience, Mayo Clinic – sequence: 8 givenname: Jennifer surname: Gass fullname: Gass, Jennifer organization: Department of Neuroscience, Mayo Clinic – sequence: 9 givenname: Melissa E orcidid: 0000-0001-7379-2545 surname: Murray fullname: Murray, Melissa E organization: Department of Neuroscience, Mayo Clinic – sequence: 10 givenname: Mitsuru surname: Shinohara fullname: Shinohara, Mitsuru organization: Department of Neuroscience, Mayo Clinic – sequence: 11 givenname: Wen-Lang surname: Lin fullname: Lin, Wen-Lang organization: Department of Neuroscience, Mayo Clinic – sequence: 12 givenname: Aliesha surname: Garrett fullname: Garrett, Aliesha organization: Department of Neuroscience, Mayo Clinic – sequence: 13 givenname: Jeannette N surname: Stankowski fullname: Stankowski, Jeannette N organization: Department of Neuroscience, Mayo Clinic – sequence: 14 givenname: Lillian surname: Daughrity fullname: 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fullname: Wang, Zizhao S organization: Department of Neuroscience, Mayo Clinic – sequence: 22 givenname: Amanda M surname: Liesinger fullname: Liesinger, Amanda M organization: Department of Neuroscience, Mayo Clinic – sequence: 23 givenname: Jeremy D surname: Baker fullname: Baker, Jeremy D organization: Department of Molecular Medicine, College of Medicine, Byrd Alzheimer's Institute, University of South Florida – sequence: 24 givenname: Jie surname: Jiang fullname: Jiang, Jie organization: Ludwig Institute, University of California at San Diego – sequence: 25 givenname: Clotilde surname: Lagier-Tourenne fullname: Lagier-Tourenne, Clotilde organization: Massachusetts General Hospital, Harvard Medical School – sequence: 26 givenname: Dieter orcidid: 0000-0002-7186-4653 surname: Edbauer fullname: Edbauer, Dieter organization: German Center for Neurodegenerative Diseases (DZNE), Institute for Metabolic Biochemistry, Ludwig Maximilians University Munich, Munich Cluster of Systems Neurology (SyNergy) – sequence: 27 givenname: Don W surname: Cleveland fullname: Cleveland, Don W organization: Ludwig Institute, University of California at San Diego, Department of Cellular and Molecular Medicine, University of California at San Diego – sequence: 28 givenname: Rosa surname: Rademakers fullname: Rademakers, Rosa organization: Department of Neuroscience, Mayo Clinic – sequence: 29 givenname: Kevin B surname: Boylan fullname: Boylan, Kevin B organization: Department of Neurology, Mayo Clinic – sequence: 30 givenname: Guojun surname: Bu fullname: Bu, Guojun organization: Department of Neuroscience, Mayo Clinic – sequence: 31 givenname: Christopher D surname: Link fullname: Link, Christopher D organization: Integrative Physiology, Institute for Behavioral Genetics, University of Colorado – sequence: 32 givenname: Chad A surname: Dickey fullname: Dickey, Chad A organization: Department of Molecular Medicine, College of Medicine, Byrd Alzheimer's Institute, University of South Florida – sequence: 33 givenname: Jeffrey D orcidid: 0000-0003-2001-8470 surname: Rothstein fullname: Rothstein, Jeffrey D organization: Department of Neurology, School of Medicine, Johns Hopkins University, Brain Science Institute, School of Medicine, Johns Hopkins University, Department of Neuroscience, School of Medicine, Johns Hopkins University – sequence: 34 givenname: Dennis W orcidid: 0000-0001-7189-7917 surname: Dickson fullname: Dickson, Dennis W organization: Department of Neuroscience, Mayo Clinic – sequence: 35 givenname: John D surname: Fryer fullname: Fryer, John D organization: Department of Neuroscience, Mayo Clinic, Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine – sequence: 36 givenname: Leonard surname: Petrucelli fullname: Petrucelli, Leonard email: petrucelli.leonard@mayo.edu organization: Department of Neuroscience, Mayo Clinic |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/26998601$$D View this record in MEDLINE/PubMed |
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| Snippet | Zhang
et al
. show that the poly(GA) proteins produced in patients with
C9ORF72
repeat expansions cause neurodegeneration and behavioral abnormalities when... Neuronal inclusions of poly(GA), a protein unconventionally translated from G4C2 repeat expansions in C9ORF72, are abundant in patients with frontotemporal... Neuronal inclusions of poly(GA), a protein unconventionally translated from [G.sub.4][C.sub.2] repeat expansions in C9ORF72, are abundant in patients with... Neuronal inclusions of poly(GA), a protein unconventionally translated from G4 C2 repeat expansions in C9ORF72, are abundant in patients with frontotemporal... Neuronal inclusions of poly(GA), a protein unconventionally translated from G sub(4)C sub(2) repeat expansions in C9ORF72, are abundant in patients with... Neuronal inclusions of poly(GA), a protein unconventionally translated from G 4 C 2 repeat expansions in C9ORF72 , are abundant in patients with frontotemporal... |
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| SubjectTerms | 14/19 631/378 64/60 692/699/375/365 82/1 82/29 82/80 96/35 Amyotrophic lateral sclerosis Amyotrophic Lateral Sclerosis - metabolism Amyotrophic Lateral Sclerosis - pathology Animal Genetics and Genomics Animals Atrophy - pathology Behavior, Animal Behavioral Sciences Biological Techniques Biomedicine Brain - metabolism Brain - pathology Brain - ultrastructure C9orf72 Protein Carrier proteins Carrier Proteins - metabolism Disease Disease susceptibility DNA-Binding Proteins - metabolism Frontotemporal Dementia - metabolism Frontotemporal Dementia - pathology Gene Expression - genetics Genetic aspects Guanine Nucleotide Exchange Factors - metabolism Humans Inclusion Bodies - metabolism Inclusion Bodies - ultrastructure Medicine Mice Mutation Nerve Degeneration - pathology Neurobiology Neurodegeneration Neurology Neurons - metabolism Neurons - pathology Neuropathology Neurosciences Open reading frames Pathology Primary Cell Culture Properties Proteins Proteins - genetics Proteins - metabolism Proteins - toxicity Toxicity Ubiquitinated Proteins - metabolism |
| Title | C9ORF72 poly(GA) aggregates sequester and impair HR23 and nucleocytoplasmic transport proteins |
| URI | https://link.springer.com/article/10.1038/nn.4272 https://www.ncbi.nlm.nih.gov/pubmed/26998601 https://www.proquest.com/docview/1784356155 https://www.proquest.com/docview/1785213478 https://www.proquest.com/docview/1787977712 https://pubmed.ncbi.nlm.nih.gov/PMC5138863 |
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