Talin and kindlin: the one-two punch in integrin activation.
Abstract Proper cell-cell and cell-matrix contacts mediated by integrin adhesion receptors are important for development, immune response, hemostasis and wound healing. Integrins pass trans-membrane signals bidirectionally through their regulated affinities for extracellular ligands and intracellular signaling molecules. Such bidirectional signaling by integrins is enabled by the conformational changes that are often linked among extracellular, transmembrane and cytoplasmic domains. Here, we review how talin-integrin and kindlin-integrin interactions, in cooperation with talin-lipid and kindlin-lipid interactions, regulate integrin affinities and how the progress in these areas helps us understand integrin-related diseases.
Department of Medicine, University of California, San Diego, La Jolla, CA, 92093, USA, feye@ucsd.edu.
Feng
F
Ye
Adam K
AK
Snider
Mark H
MH
Ginsberg
D000818:Animals; D006801:Humans; D016023:Integrins / Q000502:physiology*; D008565:Membrane Proteins / Q000502:physiology; D009363:Neoplasm Proteins / Q000502:physiology; D054730:Protein Interaction Domains and Motifs / Q000502:physiology; D015398:Signal Transduction / Q000502:physiology; D016608:Talin / Q000502:physiology*
C477322:FERMT3 protein, human; D016023:Integrins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; D016608:Talin