Zasp regulates integrin activation.
JOURNAL OF CELL SCIENCE(2012)
Abstract
Integrins are heterodimeric adhesion receptors that link the extracellular matrix (ECM) to the cytoskeleton. Binding of the scaffold protein, talin, to the cytoplasmic tail of beta-integrin causes a conformational change of the extracellular domains of the integrin heterodimer, thus allowing high-affinity binding of ECM ligands. This essential process is called integrin activation. Here we report that the Z-band alternatively spliced PDZ-motif-containing protein (Zasp) cooperates with talin to activate alpha 5 beta 1 integrins in mammalian tissue culture and alpha PS2 beta PS integrins in Drosophila. Zasp is a PDZ-LIM-domain-containing protein mutated in human cardiomyopathies previously thought to function primarily in assembly and maintenance of the muscle contractile machinery. Notably, Zasp is the first protein shown to co-activate alpha 5 beta 1 integrins with talin and appears to do so in a manner distinct from known alpha IIb beta 3 integrin co-activators.
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Key words
PDZ domain protein,Zasp,Adhesion receptor,Extracellular matrix,Integrin activation,Muscle attachment
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