α-Synuclein facilitates endocytosis by elevating the steady-state levels of phosphatidylinositol 4,5-bisphosphate.
Clathrin-mediated endocytosis
alpha-synuclein (α-synuclein)
clathrin
endocytosis
phosphoinositide
phosphoinositides
phosphorylated AP2
synapse
synaptic vesicles cycling
α-Synuclein
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:
24
07
2020
revised:
08
10
2020
pubmed:
23
10
2020
medline:
26
3
2021
entrez:
22
10
2020
Statut:
ppublish
Résumé
α-Synuclein (α-Syn) is a protein implicated in the pathogenesis of Parkinson's disease (PD). It is an intrinsically disordered protein that binds acidic phospholipids. Growing evidence supports a role for α-Syn in membrane trafficking, including, mechanisms of endocytosis and exocytosis, although the exact role of α-Syn in these mechanisms is currently unclear. Here we investigate the associations of α-Syn with the acidic phosphoinositides (PIPs), phosphatidylinositol 4,5-bisphosphate (PI(4,5)P
Identifiants
pubmed: 33087443
pii: S0021-9258(17)50683-3
doi: 10.1074/jbc.RA120.015319
pmc: PMC7939461
pii:
doi:
Substances chimiques
Adaptor Protein Complex 2
0
Clathrin
0
Phosphatidylinositol 4,5-Diphosphate
0
alpha-Synuclein
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
18076-18090Informations de copyright
© 2020 Schechter et al.
Déclaration de conflit d'intérêts
Conflict of interest—The authors declare that they have no conflict of interest with the contents of this article.
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