spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search    

The fully linked HTML version of this article has now been published.
JCS ePress online publication date 2 Mar 2004
doi: 10.1242/jcs.00987

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.00987v1
117/8/1431    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chandhoke, S. K.
Right arrow Articles by Blystone, S. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chandhoke, S. K.
Right arrow Articles by Blystone, S. D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

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.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
Md. M. Aziz, S. Ishihara, Y. Mishima, N. Oshima, I. Moriyama, T. Yuki, Y. Kadowaki, M. A. K. Rumi, Y. Amano, and Y. Kinoshita
MFG-E8 Attenuates Intestinal Inflammation in Murine Experimental Colitis by Modulating Osteopontin-Dependent {alpha}v{beta}3 Integrin Signaling
J. Immunol., June 1, 2009; 182(11): 7222 - 7232.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
W. Feng, N. P. McCabe, G. H. Mahabeleshwar, P. R. Somanath, D. R. Phillips, and T. V. Byzova
The angiogenic response is dictated by {beta}3 integrin on bone marrow-derived cells
J. Cell Biol., December 15, 2008; 183(6): 1145 - 1157.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. L. Oxley, N. J. Anthis, E. D. Lowe, I. Vakonakis, I. D. Campbell, and L. Wegener
An Integrin Phosphorylation Switch: THE EFFECT OF {beta}3 INTEGRIN TAIL PHOSPHORYLATION ON DOK1 AND TALIN BINDING
J. Biol. Chem., February 29, 2008; 283(9): 5420 - 5426.
[Abstract] [Full Text] [PDF]

Home page
 Circ. Res.Home page
G. H. Mahabeleshwar, W. Feng, K. Reddy, E. F. Plow, and T. V. Byzova
Mechanisms of Integrin Vascular Endothelial Growth Factor Receptor Cross-Activation in Angiogenesis
Circ. Res., September 14, 2007; 101(6): 570 - 580.
[Abstract] [Full Text] [PDF]

Home page
 JEMHome page
G. H. Mahabeleshwar, W. Feng, D. R. Phillips, and T. V. Byzova
Integrin signaling is critical for pathological angiogenesis
J. Exp. Med., October 30, 2006; 203(11): 2495 - 2507.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Butler and S. D. Blystone
Tyrosine Phosphorylation of {beta}3 Integrin Provides a Binding Site for Pyk2
J. Biol. Chem., April 15, 2005; 280(15): 14556 - 14562.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Gao, E. Schaefer, M. Lakkis, and S. D. Blystone
{beta}3 Tyrosine Phosphorylation and {alpha}v{beta}3-mediated Adhesion Are Required for Vav1 Association and Rho Activation in Leukocytes
J. Biol. Chem., April 15, 2005; 280(15): 15422 - 15429.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2004