Journal
JOURNAL OF CELL BIOLOGY
Volume 172, Issue 2, Pages 169-175Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200505131
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Funding
- NHLBI NIH HHS [HL41793, P01 HL045100, F32 HL010381, P01 HL006350, 1-PO1-HL45100, 2-PO1-HL06350, F32 HL10381, R01 HL041793] Funding Source: Medline
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In response to agonist stimulation, the alpha IIb beta 3 integrin on platelets is converted to an active conformation that binds fibrinogen and mediates platelet aggregation. This process contributes to both normal hemostasis and thrombosis. Activation of alpha IIb beta 3 is believed to occur in part via engagement of the beta 3 cytoplasmic tail with talin; however, the role of the alpha IIb tail and its potential binding partners in regulating alpha IIb beta 3 activation is less clear. We report that calcium and integrin binding protein 1 (CIB1), which interacts directly with the alpha IIb tail, is an endogenous inhibitor of alpha IIb beta 3 activation; overexpression of CIB1 in megakaryocytes blocks agonist-induced alpha IIb beta 3 activation, whereas reduction of endogenous CIB1 via RNA interference enhances activation. CIB1 appears to inhibit integrin activation by competing with talin for binding to alpha IIb beta 3, thus providing a model for tightly controlled regulation of alpha IIb beta 3 activation.
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