Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Biochem Biophys Res Commun. 2001 Feb 2;280(4):1085-92.

Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125.

Author information

  • 1Third Department of Internal Medicine, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minamiku, Hiroshima, 734-8551, Japan.

Abstract

alpha-Synuclein is a presynaptic protein of unknown function that has been implicated in the pathogenesis of several neurodegenerative diseases, including Parkinson's and Alzheimer's diseases. To gain insight into the functions of alpha-synuclein, we sought protein kinases that phosphorylate alpha-synuclein in the central nervous system. In contrast to Lyn, PYK2, FAK, MAPK/ERK1, SAPK/JNK, and Cdk5, only Fyn could phosphorylate alpha-synuclein. In addition, A30P and A53T mutations did not affect the phosphorylation of alpha-synuclein by Fyn. Mutation analysis revealed that activated Fyn phosphorylates specifically tyrosine residue 125 of alpha-synuclein. The distribution of alpha-synuclein and Fyn expression was similar in various parts of the brain and was colocalized in subcellular structures. Since Fyn regulates various signal transduction pathways in the central nervous system and plays an essential role in the neuronal cell differentiation, survival, and plasticity, results of this paper indicate that phosphorylation of alpha-synuclein might be involved in one of the Fyn-mediated signaling pathways in neuronal cells.

Copyright 2001 Academic Press.

PMID:
11162638
[PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances

Publication Types

MeSH Terms

Substances

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk