跳转至内容
Merck
  • Kindlin-2 phosphorylation by Src at Y193 enhances Src activity and is involved in Migfilin recruitment to the focal adhesions.

Kindlin-2 phosphorylation by Src at Y193 enhances Src activity and is involved in Migfilin recruitment to the focal adhesions.

FEBS letters (2015-06-04)
Zhaoli Liu, Danyu Lu, Xiang Wang, Junhu Wan, Chang Liu, Hongquan Zhang
摘要

Kindlin-2 regulates external to internal cell signaling by interaction with integrins in a process that involves the tyrosine kinase, Src. However, the underlying mechanisms remain elusive. Here we report that Src binds to and phosphorylates Kindlin-2 at Y193. Reciprocally, Kindlin-2-Y193 phosphorylation activates and maintains Src kinase activity. Kindlin-2-Y193 phosphorylation is also involved in its binding capacity with Migfilin and the recruitment of Migfilin to the focal adhesions. Functionally, we demonstrate that Kindlin-2-Y193 phosphorylation regulates Kindlin-2-mediated cell spreading and migration. These findings suggest that Src, Kindlin-2 and Migfilin together constitute a positive feedback loop that controls Src activity and regulates integrin-mediated cellular functions.

材料
货号
品牌
产品描述

Sigma-Aldrich
L -还原型谷胱甘肽, suitable for cell culture, BioReagent, ≥98.0%, powder
Sigma-Aldrich
L -还原型谷胱甘肽, ≥98.0%
Sigma-Aldrich
氢硫酸, ≥99.5%
Sigma-Aldrich
氢硫酸 溶液, 0.8 M in THF
Sigma-Aldrich
L -还原型谷胱甘肽, BioXtra, ≥98.0%
Sigma-Aldrich
PP2, ≥98% (HPLC)
Sigma-Aldrich
DL-酪氨酸, 99%
Sigma-Aldrich
硫-32S, 99.9 atom % 32S
Sigma-Aldrich
MISSION® esiRNA, targeting mouse Fermt2