Tau seeds are subject to aberrant modifications resulting in distinct signatures
The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer’s disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associat...
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| Published in | Cell reports (Cambridge) Vol. 35; no. 4; p. 109037 |
|---|---|
| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
27.04.2021
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| Subjects | |
| Online Access | Get full text |
| ISSN | 2211-1247 2211-1247 |
| DOI | 10.1016/j.celrep.2021.109037 |
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| Abstract | The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer’s disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associated P301L tau seeds by using in vitro and neuronal assays. We show that P301L seeds are uniquely modified by post-translational modifications (PTMs) within the microtubule-binding region (MTBR). Although these modifications do not alter tau seed trafficking or localization, acetylated tau variants show accelerated tau aggregation, enhanced tau PTM priming, and prion-like templating. To explain the enhanced tau seed acetylation, we demonstrate that P301L seeds undergo auto-acetylation. Moreover, tau acts generally to inhibit HDAC6 deacetylase activity by preventing HDAC6 phosphorylation, leading to increased substrate acetylation. Our study highlights complex post-translational regulation of transmissible tau seeds and provides insight into the biological properties of tau strains in AD and other tauopathies.
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•Tau seeds are internalized and aberrantly modified in neurons•Acetylated tau seeds display pathological properties•HDAC6 is associated with and inhibited by tau seeds•Tau prevents HDAC6 phosphorylation on Ser-22
Tseng et al. show tau seeds are abnormally processed when internalized into neurons. Tau seeds undergo a series of modifications that result as a consequence of auto-acetylation events as well as inhibition of the deacetylase HDAC6. Tau acts as an HDAC6 inhibitor by preventing HDAC6 phosphorylation at Ser-22. |
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| AbstractList | The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer’s disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associated P301L tau seeds by using in vitro and neuronal assays. We show that P301L seeds are uniquely modified by post-translational modifications (PTMs) within the microtubule-binding region (MTBR). Although these modifications do not alter tau seed trafficking or localization, acetylated tau variants show accelerated tau aggregation, enhanced tau PTM priming, and prion-like templating. To explain the enhanced tau seed acetylation, we demonstrate that P301L seeds undergo auto-acetylation. Moreover, tau acts generally to inhibit HDAC6 deacetylase activity by preventing HDAC6 phosphorylation, leading to increased substrate acetylation. Our study highlights complex post-translational regulation of transmissible tau seeds and provides insight into the biological properties of tau strains in AD and other tauopathies.
[Display omitted]
•Tau seeds are internalized and aberrantly modified in neurons•Acetylated tau seeds display pathological properties•HDAC6 is associated with and inhibited by tau seeds•Tau prevents HDAC6 phosphorylation on Ser-22
Tseng et al. show tau seeds are abnormally processed when internalized into neurons. Tau seeds undergo a series of modifications that result as a consequence of auto-acetylation events as well as inhibition of the deacetylase HDAC6. Tau acts as an HDAC6 inhibitor by preventing HDAC6 phosphorylation at Ser-22. The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer's disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associated P301L tau seeds by using in vitro and neuronal assays. We show that P301L seeds are uniquely modified by post-translational modifications (PTMs) within the microtubule-binding region (MTBR). Although these modifications do not alter tau seed trafficking or localization, acetylated tau variants show accelerated tau aggregation, enhanced tau PTM priming, and prion-like templating. To explain the enhanced tau seed acetylation, we demonstrate that P301L seeds undergo auto-acetylation. Moreover, tau acts generally to inhibit HDAC6 deacetylase activity by preventing HDAC6 phosphorylation, leading to increased substrate acetylation. Our study highlights complex post-translational regulation of transmissible tau seeds and provides insight into the biological properties of tau strains in AD and other tauopathies. The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer’s disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associated P301L tau seeds by using in vitro and neuronal assays. We show that P301L seeds are uniquely modified by post-translational modifications (PTMs) within the microtubule-binding region (MTBR). Although these modifications do not alter tau seed trafficking or localization, acetylated tau variants show accelerated tau aggregation, enhanced tau PTM priming, and prion-like templating. To explain the enhanced tau seed acetylation, we demonstrate that P301L seeds undergo auto-acetylation. Moreover, tau acts generally to inhibit HDAC6 deacetylase activity by preventing HDAC6 phosphorylation, leading to increased substrate acetylation. Our study highlights complex post-translational regulation of transmissible tau seeds and provides insight into the biological properties of tau strains in AD and other tauopathies. Tseng et al. show tau seeds are abnormally processed when internalized into neurons. Tau seeds undergo a series of modifications that result as a consequence of auto-acetylation events as well as inhibition of the deacetylase HDAC6. Tau acts as an HDAC6 inhibitor by preventing HDAC6 phosphorylation at Ser-22. The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer's disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associated P301L tau seeds by using in vitro and neuronal assays. We show that P301L seeds are uniquely modified by post-translational modifications (PTMs) within the microtubule-binding region (MTBR). Although these modifications do not alter tau seed trafficking or localization, acetylated tau variants show accelerated tau aggregation, enhanced tau PTM priming, and prion-like templating. To explain the enhanced tau seed acetylation, we demonstrate that P301L seeds undergo auto-acetylation. Moreover, tau acts generally to inhibit HDAC6 deacetylase activity by preventing HDAC6 phosphorylation, leading to increased substrate acetylation. Our study highlights complex post-translational regulation of transmissible tau seeds and provides insight into the biological properties of tau strains in AD and other tauopathies.The prion-like spread of tau pathology could underlie a spectrum of clinical syndromes including Alzheimer's disease (AD). Although evidence indicates that tau is transmissible, it is unclear how pathogenic tau seeds are processed in neurons. Here, we analyze fibrillar wild-type and disease-associated P301L tau seeds by using in vitro and neuronal assays. We show that P301L seeds are uniquely modified by post-translational modifications (PTMs) within the microtubule-binding region (MTBR). Although these modifications do not alter tau seed trafficking or localization, acetylated tau variants show accelerated tau aggregation, enhanced tau PTM priming, and prion-like templating. To explain the enhanced tau seed acetylation, we demonstrate that P301L seeds undergo auto-acetylation. Moreover, tau acts generally to inhibit HDAC6 deacetylase activity by preventing HDAC6 phosphorylation, leading to increased substrate acetylation. Our study highlights complex post-translational regulation of transmissible tau seeds and provides insight into the biological properties of tau strains in AD and other tauopathies. |
| ArticleNumber | 109037 |
| Author | Chen, Youjun Patel, Niyati Meeker, Rick B. Ajit, Aditi Rigo, Frank Tabassum, Zarin Tseng, Jui-Heng Tian, Xu Prevatte, Alex W. Ling, Karen Herring, Laura E. Cohen, Todd J. |
| AuthorAffiliation | 5 Lead contact 4 Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA 2 UNC Proteomics Core Facility, Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA 3 Ionis Pharmaceuticals, Carlsbad, CA 92008, USA 1 Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA |
| AuthorAffiliation_xml | – name: 1 Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – name: 3 Ionis Pharmaceuticals, Carlsbad, CA 92008, USA – name: 2 UNC Proteomics Core Facility, Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA – name: 5 Lead contact – name: 4 Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA |
| Author_xml | – sequence: 1 givenname: Jui-Heng orcidid: 0000-0002-9036-9121 surname: Tseng fullname: Tseng, Jui-Heng organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 2 givenname: Aditi surname: Ajit fullname: Ajit, Aditi organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 3 givenname: Zarin orcidid: 0000-0001-9007-2566 surname: Tabassum fullname: Tabassum, Zarin organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 4 givenname: Niyati surname: Patel fullname: Patel, Niyati organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 5 givenname: Xu surname: Tian fullname: Tian, Xu organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 6 givenname: Youjun surname: Chen fullname: Chen, Youjun organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 7 givenname: Alex W. surname: Prevatte fullname: Prevatte, Alex W. organization: UNC Proteomics Core Facility, Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 8 givenname: Karen surname: Ling fullname: Ling, Karen organization: Ionis Pharmaceuticals, Carlsbad, CA 92008, USA – sequence: 9 givenname: Frank surname: Rigo fullname: Rigo, Frank organization: Ionis Pharmaceuticals, Carlsbad, CA 92008, USA – sequence: 10 givenname: Rick B. orcidid: 0000-0002-7487-5315 surname: Meeker fullname: Meeker, Rick B. organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 11 givenname: Laura E. surname: Herring fullname: Herring, Laura E. organization: UNC Proteomics Core Facility, Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 12 givenname: Todd J. orcidid: 0000-0002-4099-0278 surname: Cohen fullname: Cohen, Todd J. email: toddcohen@neurology.unc.edu organization: Department of Neurology and the UNC Neuroscience Center, University of North Carolina, Chapel Hill, NC 27599, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33910013$$D View this record in MEDLINE/PubMed |
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| Copyright | 2021 The Author(s) Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved. |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 AUTHOR CONTRIBUTIONS J.-H.T. led most aspects of the experimental study and performed the molecular, cell-based, and biochemical experiments. A.A., Z.T., and N.P. provided technical assistance with immunoblotting and mass spectrometry analysis. X.T. performed molecular cloning and lentiviral production. Y.C. assisted with plasmid preparation, mouse handling, breeding, and colony maintenance. K.L. and F.R. developed and optimized HDAC6 ASOs for use in primary mouse neuron experiments. R.B.M. performed macrophage and microglia isolation and established optimal cell culture conditions. L.E.H. and A.W.P. performed mass spectrometry analyses and analyzed HDAC6 PTM data. J.-H.T. and T.J.C. co-wrote the manuscript. This study was directed and supervised by T.J.C. |
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| Title | Tau seeds are subject to aberrant modifications resulting in distinct signatures |
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