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Ubiquitination of protein Tau in Alzheimer's disease

ABSTRACT: Identification of posttranlational modifications of Tau in Alzheimer's disease

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Brain

SUBMITTER: Yingxin Zhao

LAB HEAD: Yingxin Zhao, Ph.D.

PROVIDER: PXD031417 | Pride | 2022-05-19

REPOSITORIES: Pride

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Lysine 63-linked ubiquitination of tau oligomers contributes to the pathogenesis of Alzheimer's disease.

Puangmalai Nicha N Sengupta Urmi U Bhatt Nemil N Gaikwad Sagar S Montalbano Mauro M Bhuyan Arijit A Garcia Stephanie S McAllen Salome S Sonawane Minal M Jerez Cynthia C Zhao Yingxin Y Kayed Rakez R

The Journal of biological chemistry 20220222 4

Ubiquitin-modified tau aggregates are abundantly found in human brains diagnosed with Alzheimer's disease (AD) and other tauopathies. Soluble tau oligomers (TauO) are the most neurotoxic tau species that propagate pathology and elicit cognitive deficits, but whether ubiquitination contributes to tau formation and spreading is not fully understood. Here, we observed that K63-linked, but not K48-linked, ubiquitinated TauO accumulated at higher levels in AD brains compared with age-matched controls ...[more]

PMID: 35202653

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