Src phosphorylation of cortactin enhances actin assembly

被引：182
|
作者：
Tehrani, Shandiz
Tomasevic, Nenad
Weed, Scott
Sakowicz, Roman
Cooper, John A.
机构：
[1] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA
[2] Cytokinet Inc, San Francisco, CA 94080 USA
[3] W Virginia Univ, Mary Babb Randolph Canc Ctr, Morgantown, WV 26506 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2007年 / 104卷 / 29期
关键词：
N-WASp; Nck; tyrosine phosphorylation;
D O I：
10.1073/pnas.0701077104
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Src kinase mediates growth factor signaling and causes oncogenic transformation, which includes dramatic changes in the actin cytoskeleton, cell shape, and motility. Cortactin was discovered as a substrate for Src. How phosphorylation of cortactin can enhance actin assembly is unknown. Here, using an actin assembly system reconstituted from purified components, we demonstrate for the first time a biochemical mechanism by which Src phosphorylation of cortactin affects actin assembly. The adaptor Nck is an important component of the system, linking phosphorylated cortactin with neuronal WASp (N-WASp) and WASp-interacting protein (WIP) to activate Arp2/3 complex.
引用
收藏
页码：11933 / 11938
页数：6
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