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J. Biol. Chem., Vol. 280, Issue 15, 14556-14562, April 15, 2005

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Tyrosine Phosphorylation of ₃ Integrin Provides a Binding Site for Pyk2^*

Boyd Butler and Scott D. Blystone

From the Department of Cell and Developmental Biology, SUNY Upstate Medical University, Syracuse, New York 13210

Integrins expressed on leukocytes possess the ability to maintain themselves in a non-adhesive state, thus preventing unwarranted adhesion and uncontrolled inflammation. Leukocyte adhesion is regulated through the modulation of integrin receptors such as _V3. Firm adhesion to the extracellular matrix and directed cellular motility requires the reorganization of the actin cytoskeleton. The ability of ₃ to recruit signaling and scaffolding molecules to propagate _V3 -mediated signals is regulated in part by the phosphorylation of the ₃ cytoplasmic tail. The identities of integrin-associated signaling molecules within _V3 podosomes and in particular the proximal binding partners of the ₃ cytoplasmic tail are not completely known. Here we show that _V3 ligation induces Pyk2-Tyr-402 phosphorylation and its association with the ₃ cytoplasmic tail in a ₃-Tyr-747 phosphorylation-dependent manner. Pyk2 binding to the ₃ cytoplasmic tail is direct and dependent upon Pyk2-Tyr-402 and ₃ -Tyr-747 phosphorylations. These data identify Pyk2 as a phosphorylated ₃ binding partner, providing a potential structural and signaling platform to achieve _V3 -mediated remodeling of the actin cytoskeleton.

Received for publication, October 15, 2004 , and in revised form, December 23, 2004.

^* This work was supported by NIAID, National Institutes of Health Grants R01AI40602 and K02AI57384 (to S. D. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams St., Syracuse, NY 13210. Tel.: 315-464-8512; Fax: 315-464-8535; E-mail: Blystons{at}upstate.edu.

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