Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells

Stable platelet aggregation, adhesion, and spreading during hemostasis are promoted by outside-in αIIbβ3 signals that feature rapid activation of c-Src and Syk, delayed activation of FAK, and cytoskeletal reorganization. To evaluate these αIIbβ3–tyrosine kinase interactions at nanometer proximity in...

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Main Authors:	de Virgilio, Maddalena, Kiosses, William B., Shattil, Sanford J.
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2004
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172182/

id	pubmed-2172182
recordtype	oai_dc
spelling	pubmed-21721822008-03-05 Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells de Virgilio, Maddalena Kiosses, William B. Shattil, Sanford J. Article Stable platelet aggregation, adhesion, and spreading during hemostasis are promoted by outside-in αIIbβ3 signals that feature rapid activation of c-Src and Syk, delayed activation of FAK, and cytoskeletal reorganization. To evaluate these αIIbβ3–tyrosine kinase interactions at nanometer proximity in living cells, we monitored bioluminescence resonance energy transfer between GFP and Renilla luciferase chimeras and bimolecular fluorescence complementation between YFP half-molecule chimeras. These techniques revealed that αIIbβ3 interacts with c-Src at the periphery of nonadherent CHO cells. After plating cells on fibrinogen, complexes of αIIbβ3–c-Src, αIIbβ3–Syk, and c-Src–Syk are observed in membrane ruffles and focal complexes, and the interactions involving Syk require Src activity. In contrast, FAK interacts with αIIbβ3 and c-Src, but not with Syk, in focal complexes and adhesions. All of these interactions require the integrin β3 cytoplasmic tail. Thus, αIIbβ3 interacts proximally, if not directly, with tyrosine kinases in a coordinated, selective, and dynamic manner during sequential phases of αIIbβ3 signaling to the actin cytoskeleton. The Rockefeller University Press 2004-05-10 /pmc/articles/PMC2172182/ /pubmed/15123737 http://dx.doi.org/10.1083/jcb.200402064 Text en Copyright © 2004, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	de Virgilio, Maddalena Kiosses, William B. Shattil, Sanford J.
spellingShingle	de Virgilio, Maddalena Kiosses, William B. Shattil, Sanford J. Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
author_facet	de Virgilio, Maddalena Kiosses, William B. Shattil, Sanford J.
author_sort	de Virgilio, Maddalena
title	Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
title_short	Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
title_full	Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
title_fullStr	Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
title_full_unstemmed	Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells
title_sort	proximal, selective, and dynamic interactions between integrin αiibβ3 and protein tyrosine kinases in living cells
description	Stable platelet aggregation, adhesion, and spreading during hemostasis are promoted by outside-in αIIbβ3 signals that feature rapid activation of c-Src and Syk, delayed activation of FAK, and cytoskeletal reorganization. To evaluate these αIIbβ3–tyrosine kinase interactions at nanometer proximity in living cells, we monitored bioluminescence resonance energy transfer between GFP and Renilla luciferase chimeras and bimolecular fluorescence complementation between YFP half-molecule chimeras. These techniques revealed that αIIbβ3 interacts with c-Src at the periphery of nonadherent CHO cells. After plating cells on fibrinogen, complexes of αIIbβ3–c-Src, αIIbβ3–Syk, and c-Src–Syk are observed in membrane ruffles and focal complexes, and the interactions involving Syk require Src activity. In contrast, FAK interacts with αIIbβ3 and c-Src, but not with Syk, in focal complexes and adhesions. All of these interactions require the integrin β3 cytoplasmic tail. Thus, αIIbβ3 interacts proximally, if not directly, with tyrosine kinases in a coordinated, selective, and dynamic manner during sequential phases of αIIbβ3 signaling to the actin cytoskeleton.
publisher	The Rockefeller University Press
publishDate	2004
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2172182/
_version_	1611424842596220928

Proximal, selective, and dynamic interactions between integrin αIIbβ3 and protein tyrosine kinases in living cells

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