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First published online 2 March 2004
doi: 10.1242/jcs.00987

Journal of Cell Science 117, 1431-1441 (2004)
Published by The Company of Biologists 2004
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Research Article

ß3 integrin phosphorylation is essential for Arp3 organization into leukocyte {alpha}Vß3-vitronectin adhesion contacts

Surjit K. Chandhoke1, Matthew Williams1, Erik Schaefer2, Linda Zorn2 and Scott D. Blystone1,*

1 Department of Cell and Developmental Biology SUNY Upstate Medical University, 750 East Adams St, Syracuse, NY 13210, USA
2 Biosource International, Hopkinton, MA 01748, USA

* Author for correspondence (e-mail: blystons{at}mail.upstate.edu)

Accepted 13 November 2003

Integrins play a pivotal role in self-regulated hematopoietic adhesion and migration. Leukocyte {alpha}Vß3 integrin-mediated adhesion to vitronectin requires protein kinase C activation and phosphorylation on tyrosine 747 of the ß3 cytoplasmic tail. We have previously shown that ß3 phosphorylation is required for Rho activation. In this study, an antibody specific to phosphorylated ß3 tyrosine 747 was used to localize phosphorylated {alpha}Vß3 in vitronectin adhesive structures. Early adhesion contacts containing phosphorylated ß3 preceded actin stress fiber formation. ß3 phosphorylation decreased progressively throughout the course of adhesion coincident with the appearance of actin stress fibers. Time-dependent increases in colocalization of ß3 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 ß3 but not in those expressing a nonphosphorylatable mutant of ß3, suggesting that ß3 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 ß3 phosphorylation throughout the adhesion time course. These data confirm a requirement for ß3 phosphorylation in {alpha}Vß3-mediated adhesion to vitronectin and suggest that ß3 phosphorylation permits signaling complex assembly at the adhesion site necessary for actin stress fiber formation in leukocytes.

Key words: Cytoskeleton, PSSA, Pyk2, Actin




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