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JCS ePress online publication date 2 Mar 2004
doi: 10.1242/jcs.00987

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Research Article

{beta}3 integrin phosphorylation is essential for Arp3 organization into leukocyte {alpha}V{beta}3-vitronectin adhesion contacts


Surjit K. Chandhoke, Matthew Williams, Erik Schaefer, Linda Zorn, and Scott D. Blystone*
* Author for correspondence (e-mail: blystons{at}mail.upstate.edu)

Integrins play a pivotal role in self-regulated hematopoietic adhesion and migration. Leukocyte {alpha}V{beta}3 integrin-mediated adhesion to vitronectin requires protein kinase C activation and phosphorylation on tyrosine 747 of the {beta}3 cytoplasmic tail. We have previously shown that {beta}3 phosphorylation is required for Rho activation. In this study, an antibody specific to phosphorylated {beta}3 tyrosine 747 was used to localize phosphorylated {alpha}V{beta}3 in vitronectin adhesive structures. Early adhesion contacts containing phosphorylated {beta}3 preceded actin stress fiber formation. {beta}3 phosphorylation decreased progressively throughout the course of adhesion coincident with the appearance of actin stress fibers. Time-dependent increases in colocalization of {beta}3 with tyrosine 402 phosphorylated Pyk2 in similar adhesive structures was observed, providing evidence for downstream signaling complex formation. Surprisingly, Arp3 organized into similar adhesion contacts in cells expressing wild-type {beta}3 but not in those expressing a nonphosphorylatable mutant of {beta}3, suggesting that {beta}3 phosphorylation is required for sequestration of Arp3 to adhesion complexes. Suppression of actin stress fiber formation by an inhibitor to Rho kinase disrupted Arp3 organization while prolonging {beta}3 phosphorylation throughout the adhesion time course. These data confirm a requirement for {beta}3 phosphorylation in {alpha}V{beta}3-mediated adhesion to vitronectin and suggest that {beta}3 phosphorylation permits signaling complex assembly at the adhesion site necessary for actin stress fiber formation in leukocytes.
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