Kindlin and Integrin Activation

Abstract: Bidirectional integrin signaling mediates cell-extracellular matrix， cell-cell adhesion and cell migration. Mechanisms have been established whereby the FERM domain in the N-terminal region of talin binding to the membrane-proximal NPxY motif in the integrin β cytoplasmic domian constitutes a final common step of signaling leading to integrin activation. Recent studies have shown that the interactions between FERM domain in the C-terminal region of kindlins and the membrane-distal NxxY motif in the integrin β cytoplasmic domain synergize with talin to activate integrin. There are three mammalian kindlins including kindlin-1， kindlin-2， kindlin-3 and the three human kindlins exhibit a high homology in amino acid sequence and an identical domain architecture as well. This review summarizes the distribution， domain structure and molecular activities of kindlins and provides a current overview of the roles of kindlins in integrin activation.

CSTR: 32200.14.cjcb.2010.04.0024