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. 2006 Feb 3;21(3):337-47.
doi: 10.1016/j.molcel.2006.01.011.

The molecular basis of filamin binding to integrins and competition with talin

Tiila Kiema  1 , Yatish Lad, Pengju Jiang, Camilla L Oxley, Massimiliano Baldassarre, Kate L Wegener, Iain D Campbell, Jari Ylänne, David A Calderwood
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Free article

The molecular basis of filamin binding to integrins and competition with talin

Tiila Kiema et al. Mol Cell. .
Free article

Abstract

The ability of adhesion receptors to transmit biochemical signals and mechanical force across cell membranes depends on interactions with the actin cytoskeleton. Filamins are large, actin-crosslinking proteins that connect multiple transmembrane and signaling proteins to the cytoskeleton. Here, we describe the high-resolution structure of an interface between filamin A and an integrin adhesion receptor. When bound, the integrin beta cytoplasmic tail forms an extended beta strand that interacts with beta strands C and D of the filamin immunoglobulin-like domain (IgFLN) 21. This interface is common to many integrins, and we suggest it is a prototype for other IgFLN domain interactions. Notably, the structurally defined filamin binding site overlaps with that of the integrin-regulator talin, and these proteins compete for binding to integrin tails, allowing integrin-filamin interactions to impact talin-dependent integrin activation. Phosphothreonine-mimicking mutations inhibit filamin, but not talin, binding, indicating that kinases may modulate this competition and provide additional means to control integrin functions.

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