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Published online May 5, 2008
doi:10.1083/jcb.200710196
The Journal of Cell Biology, Vol. 181, No. 3, 439-446
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Ma et al.
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Report

 Kindlin-2 (Mig-2): a co-activator of β3 integrins

Yan-Qing Ma1, Jun Qin1, Chuanyue Wu2, and Edward F. Plow1

1 Department of Molecular Cardiology, Cleveland Clinic, Cleveland, OH 44195
2 Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261

Correspondence to Edward F. Plow: plowe{at}ccf.org

Integrin activation is essential for dynamically linking the extracellular environment and cytoskeletal/signaling networks. Activation is controlled by integrins' short cytoplasmic tails (CTs). It is widely accepted that the head domain of talin (talin-H) can mediate integrin activation by binding to two sites in integrin β's CT; in integrin β3 this is an NPLY747 motif and the membrane-proximal region. Here, we show that the C-terminal region of integrin β3 CT, composed of a conserved TS752T region and NITY759 motif, supports integrin activation by binding to a cytosolic binding partner, kindlin-2, a widely distributed PTB domain protein. Co-transfection of kindlin-2 with talin-H results in a synergistic enhancement of integrin {alpha}IIbβ3 activation. Furthermore, siRNA knockdown of endogenous kindlin-2 impairs talin-induced {alpha}IIbβ3 activation in transfected CHO cells and blunts {alpha}vβ3-mediated adhesion and migration of endothelial cells. Our results thus identify kindlin-2 as a novel regulator of integrin activation; it functions as a coactivator.

Abbreviations used in this paper: CT, cytoplasmic tail; HUVEC, human umbilical vein endothelial cell; talin-H, talin head domain.


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