Talin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation
Seiji Tadokoro, Sanford J. Shattil, Koji Eto, Vera Tai, Robert Liddington, José M. de Pereda, Mark H. Ginsberg, David Calderwood
Abstract
Seiji Tadokoro, Sanford J. Shattil, Koji Eto, Vera Tai, Robert Liddington, José M. de Pereda, Mark H. Ginsberg, David Calderwood
Abstract
Control of integrin affinity for ligands (integrin activation) is essential for normal cell adhesion, migration, and assembly of an extracellular matrix. Integrin activation is usually mediated through the integrin beta subunit cytoplasmic tail and can be regulated by many different biochemical signaling pathways. We report that specific binding of the cytoskeletal protein talin to integrin beta subunit cytoplasmic tails leads to the conformational rearrangements of integrin extracellular domains that increase their affinity. Thus, regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation.
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Control of integrin affinity for ligands (integrin activation) is essential for normal cell adhesion, migration, and assembly of an extracellular matrix. Integrin activation is usually mediated through the integrin beta subunit cytoplasmic tail and can be regulated by many different biochemical signaling pathways. We report that specific binding of the cytoskeletal protein talin to integrin beta subunit cytoplasmic tails leads to the conformational rearrangements of integrin extracellular domains that increase their affinity. Thus, regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation.
Key concepts: Integrin, CD49c, Integrin, beta 6, Collagen receptor, Cell biology, Integrin alpha M, Cytoplasm, Protein subunit