Activation of Pyk2/RAFTK induces tyrosine phosphorylation of α‐synuclein via Src‐family kinases

FEBS Letters

Nakamura, Shigenobu²  Nakamura, Takeshi²  Takahashi, Tetsuya²  Avraham, Hava¹  Matsumoto, Masayasu²  Nagano, Yoshito²  Avraham, Shalom¹  Yamashita, Hiroshi² 

[1] Division of Experimental Medicine, Beth Israel-Deaconess Medical Center, Harvard Institute of Medicine, 4 Blackfan Circle, Boston, MA 02115, USA;Department of Clinical Neuroscience and Therapeutics, Hiroshima University Graduate School of Biomedical Sciences, 1-2-3 Kasumi, Hiroshima 734-8551, Japan

关键词: α-Synuclein;    Tyrosine phosphorylation;    Pyk2/RAFTK;    Osmotic stress;    Parkinson's disease;   

DOI  :  10.1016/S0014-5793(02)02861-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

α-Synuclein (αS) 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 αS. Hyperosmotic stress induced tyrosine phosphorylation of αS via Pyk2/RAFTK at tyrosine residue 125. Pyk2/RAFTK-mediated phosphorylation of αS was primarily achieved with Src-family kinases. In addition, osmotic stress-induced phosphorylation of αS 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 αS.

【 授权许可】

Unknown