A combinatorial native MS and LC-MS/MS approach reveals high intrinsic phosphorylation of human Tau but minimal levels of other key modifications.
Alzheimer's disease
LC-MS
Tau protein (Tau)
mass spectrometry (MS)
native mass spectrometry
phosphorylation
protein aggregation
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:
25 12 2020
25 12 2020
Historique:
received:
02
09
2020
revised:
21
10
2020
pubmed:
28
10
2020
medline:
24
3
2021
entrez:
27
10
2020
Statut:
ppublish
Résumé
Abnormal changes of neuronal Tau protein, such as phosphorylation and aggregation, are considered hallmarks of cognitive deficits in Alzheimer's disease. Abnormal phosphorylation is thought to precede aggregation and therefore to promote aggregation, but the nature and extent of phosphorylation remain ill-defined. Tau contains ∼85 potential phosphorylation sites, which can be phosphorylated by various kinases because the unfolded structure of Tau makes them accessible. However, methodological limitations (
Identifiants
pubmed: 33106314
pii: S0021-9258(17)50693-6
doi: 10.1074/jbc.RA120.015882
pmc: PMC7939451
pii:
doi:
Substances chimiques
tau Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
18213-18225Informations de copyright
© 2020 Drepper et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.
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