The Cytoplasmic Domain of αIIbβ3
نویسندگان
چکیده
منابع مشابه
Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK
pp125FAK (focal adhesion kinase) a protein tyrosine kinase that may mediate cellular responses to adhesion, is activated and tyrosine-phosphorylated when platelets adhere to fibrinogen via the integrin, αIIbβ3. To determine whether either of the cytoplasmic tails of αIIbβ3 regulates FAK phosphorylation, CHO cells were stably transfected with αIIbβ3 or various cytoplasmic tail truncation mutants...
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which induces cascades of intracellular signaling events, including protein phosphorylation and cytoskel-etal reorganization (Schwartz et al., 1995; Shattil and Ginsberg, 1997). However, ligand binding to integrins is not simply controlled by ligand availability but also through " inside-out " signaling: cellular stimulation clus-3 Joseph J. Jacobs Center for Thrombosis and ters integrins or al...
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The large atypical cadherin Fat is a receptor for both Hippo and planar cell polarity (PCP) pathways. Here we investigate the molecular basis for signal transduction downstream of Fat by creating targeted alterations within a genomic construct that contains the entire fat locus, and by monitoring and manipulating the membrane localization of the Fat pathway component Dachs. We establish that th...
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Agonist-stimulated platelet activation triggers conformational changes of integrin αIIbβ3, allowing fibrinogen binding and platelet aggregation. We have previously shown that an octapeptide, p1YMESRADR8, corresponding to amino acids 313-320 of the β-ribbon extending from the β-propeller domain of αIIb, acts as a potent inhibitor of platelet aggregation. Here we have performed in silico modellin...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.11.6017