Phosphorylation of p36 in vitro with pp60src

FEBS Letters

Glenney, John R.¹ 

[1] Molecular Biology and Virology Laboratory, The Salk Institute, PO Box 85800, San Diego, CA 92138, USA

关键词: Cytoskeleton;    Actin;    Tyrosine kinase;    Growth factor;   

DOI  :  10.1016/0014-5793(85)80047-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

P36 is a major substrate of the tyrosine protein kinases. P36 isolated from bovine intestine was used in phosphorylation reactions with pp60^src. Phosphorylation was stimulated 3–5-fold by Ca²⁺, however the K _m was the same (2.5μM) at high or low Ca²⁺. Although the level of free Ca²⁺ needed for this enhanced phosphorylation was 10⁻⁴–10⁻³)⁻³ M, phosphatidylserine shifted the Ca²⁺ sensitivity to the 10⁻⁶–10⁻⁵ M range. Independent evidence suggested that p36 interacts directly with liposomes containing phosphatidylserine. This raises the possibility that p36, like c-kinase, is a Ca²⁺-activated, phospholipid-dependent protein.

【 授权许可】

Unknown