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 in | Molecular cell Vol. 81; no. 20; pp. 4209 - 4227.e12 |
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Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier Inc
21.10.2021
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Subjects | |
Online Access | Get full text |
ISSN | 1097-2765 1097-4164 1097-4164 |
DOI | 10.1016/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. |
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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 |
AuthorAffiliation_xml | – name: 3 Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Rochester, MN 55905 – name: 9 Department of Pathology, Mount Sinai Medical Center, New York, NY 10029 – name: 2 Center for Network Systems Biology, Boston University School of Medicine, Boston, MA, 02118 – name: 10 Department of Electrical and Computer Engineering, Boston University, Boston, MA 02459 – name: 4 Department of Neurology, Boston University School of Medicine, Boston, MA 02118 – name: 7 Department of Translational Science and Molecular Medicine, College of Human Medicine, Michigan State University, Grand Rapids, MI 49503 – name: 6 Department of Neuroscience, University of Florida, Gainesville, FL 32611 – name: 1 Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, 02118 – name: 12 Center for Systems Neuroscience, Boston University, Boston, MA 02215 – name: 11 Center for Neurophotonics, Boston University, Boston, MA 02215 – name: 5 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824 – name: 8 Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224 |
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givenname: Jose F. surname: Abisambra fullname: Abisambra, Jose F. organization: Department of Neuroscience, University of Florida, Gainesville, FL 32611, USA – sequence: 17 givenname: Min-Hao surname: Kuo fullname: Kuo, Min-Hao organization: Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA – sequence: 18 givenname: Nicholas surname: Kanaan fullname: Kanaan, Nicholas organization: Department of Translational Science and Molecular Medicine, College of Human Medicine, Michigan State University, Grand Rapids, MI 49503, USA – sequence: 19 givenname: Melissa E. surname: Murray fullname: Murray, Melissa E. organization: Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA – sequence: 20 givenname: John F. surname: Crary fullname: Crary, John F. organization: Department of Pathology, Mount Sinai Medical Center, New York, NY 10029, USA – sequence: 21 givenname: Jian surname: Zhao fullname: Zhao, Jian organization: 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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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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Undefined-3 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. |
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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 |
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