Talin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation

By S. Tadokoro, S. Shattil, K. Eto, Vera Tai, R. Liddington, J. M. de Pereda, M. Ginsberg, D. Calderwood. Science, 2003

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Talins and kindlins; partners in integrin-mediated adhesion (2013, positive): “RIAM and lamellipodin contain a RAS-associating domain (RA domain) and an adjacent pleckstrin homolog y domain (PH domain), and the structure of the RIAM RA–PH double domain suggests that they act as a proximity detector for activated RAP1A and PtdIns(4,5)P2 (REF.”
FAK phosphorylation sites mapped by mass spectrometry (2005, background): “Binding of the integrin cytoplasmic tails to the FERM domain of talin induces conformational changes in the integrin extracellular domains, thus increasing their affinity for ligands (Calderwood et al., 2004; Tadokoro et al., 2003; Calderwood et al., 2002; Kim et al., 2003).”
Mechanical Integration of Actin and Adhesion Dynamics in Cell Migration (2010, background): “Enhanced affinity of integrin extracellular heads for the ECM, which is known as activation, occurs through association of their cytoplasmic tails with the vinculinand actin-binding protein talin (Tadokoro et al. 2003).”
Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “Talin binding is believed to represent the final common step in integrin activation (Tadokoro et al. 2003).”