Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau.

Tau protein (Tau) aggregation amyloid lipid binding microtubule neurodegenerative disease phosphorylation phosphotyrosine post-translational modification (PTM) tauopathy

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
05 06 2020
Historique:
received: 31 12 2019
revised: 22 04 2020
pubmed: 29 4 2020
medline: 29 12 2020
entrez: 29 4 2020
Statut: ppublish

Résumé

The microtubule-associated protein Tau is implicated in the pathogenesis of several neurodegenerative disorders, including Alzheimer's disease. Increasing evidence suggests that post-translational modifications play critical roles in regulating Tau's normal functions and its pathogenic properties in tauopathies. Very little is known about how phosphorylation of tyrosine residues influences the structure, aggregation, and microtubule- and lipid-binding properties of Tau. Here, we sought to determine the relative contributions of phosphorylation of one or several of the five tyrosine residues in Tau (Tyr-18, -29, -197, -310, and -394) to the regulation of its biophysical, aggregation, and functional properties. We used a combination of site-specific mutagenesis and

Identifiants

pubmed: 32341125
pii: S0021-9258(17)49432-4
doi: 10.1074/jbc.RA119.012517
pmc: PMC7278352
doi:

Substances chimiques

Lipids 0
MAPT protein, human 0
tau Proteins 0
Tyrosine 42HK56048U

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

7905-7922

Subventions

Organisme : NIA NIH HHS
ID : R37 AG019391
Pays : United States
Organisme : NIH HHS
ID : S10 OD016320
Pays : United States

Informations de copyright

© 2020 Ait-Bouziad et al.

Déclaration de conflit d'intérêts

Conflict of interest—Prof. Hilal Lashuel is the founder and chief scientific officer of ND BioSciences SA.

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Auteurs

Nadine Ait-Bouziad (N)

Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.

Anass Chiki (A)

Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.

Galina Limorenko (G)

Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.

Shifeng Xiao (S)

Shenzhen Key Laboratory of Marine Biotechnology and Ecology, College of Life Sciences and Oceanography, Shenzhen University, Shenzhen, China.
Department of Biochemistry and Program in Structural Biology, Weill Cornell Medical College, New York, New York.

David Eliezer (D)

Department of Biochemistry and Program in Structural Biology, Weill Cornell Medical College, New York, New York.

Hilal A Lashuel (HA)

Laboratory of Molecular and Chemical Biology of Neurodegeneration, Brain Mind Institute, École Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland Hilal.lashuel@epfl.ch.

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