Journal
FEBS LETTERS
Volume 589, Issue 15, Pages 2001-2010Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2015.05.038
Keywords
Src; Kindlin-2; Migfilin; Tyrosine phosphorylation; Focal adhesion
Funding
- Ministry of Science and Technology of China [2015CB553906, 2013CB910501, 2013ZX09401- 004-006]
- National Natural Science Foundation of China [81230051, 81472734, 31170711, 81321003, 30830048]
- Project of the Ministry of Education, Beijing Natural Science Foundation [7120002]
- Peking University [BMU20120314, BMU20130364]
- Leading Academic Discipline Project of Beijing Education Bureau
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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. (C) 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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