Article

Activation of Pyk2/RAFTK induces tyrosine phosphorylation of alpha-synuclein via Src-family kinases.

Department of Clinical Neuroscience and Therapeutics, Hiroshima University Graduate School of Biomedical Sciences, Japan.
FEBS Letters (impact factor: 3.54). 07/2002; 521(1-3):190-4. pp.190-4
Source: PubMed

ABSTRACT alpha-Synuclein (alpha S) is a neuronal protein that has been implicated in the pathogenesis of Parkinson's disease. The present report demonstrates that the protein tyrosine kinase Pyk2/RAFTK is involved in cell stress-induced tyrosine phosphorylation of alpha S. Hyperosmotic stress induced tyrosine phosphorylation of alpha S via Pyk2/RAFTK at tyrosine residue 125. Pyk2/RAFTK-mediated phosphorylation of alpha S was primarily achieved with Src-family kinases. In addition, osmotic stress-induced phosphorylation of alpha S was dependent on Pyk2/RAFTK activation. Accordingly, such results indicate that Pyk2/RAFTK lies upstream of Src-family kinases in the signaling cascade by which osmotic stress induces tyrosine phosphorylation of alpha S.

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Keywords

alpha S
 
alpha S. Hyperosmotic stress induced tyrosine phosphorylation
 
alpha-Synuclein
 
cell stress-induced tyrosine phosphorylation
 
osmotic stress induces tyrosine phosphorylation
 
osmotic stress-induced phosphorylation
 
Parkinson's disease
 
present report
 
protein tyrosine kinase Pyk2/RAFTK
 
Pyk2/RAFTK
 
Pyk2/RAFTK activation
 
Pyk2/RAFTK-mediated phosphorylation
 
signaling cascade
 
Src-family kinases
 
tyrosine residue 125