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lüll Platelet integrin alpha(IIb)beta(3): activation mechanisms Ma YQ; Qin J; Plow EFJ Thromb Haemost 2007[Jul]; 5 (7): 1345-52Integrin alpha(IIb)beta(3) plays a critical role in platelet aggregation, a central response in hemostasis and thrombosis. This function of alpha(IIb)beta(3) depends upon a transition from a resting to an activated state such that it acquires the capacity to bind soluble ligands. Diverse platelet agonists alter the cytoplasmic domain of alpha(IIb)beta(3) and initiate a conformational change that traverses the transmembrane region and ultimately triggers rearrangements in the extracellular domain to permit ligand binding. The membrane-proximal regions of alpha(IIb) and beta(3) cytoplasmic tails, together with the transmembrane segments of the subunits, contact each other to form a complex which restrains the integrin in the resting state. It is unclasping of this complex that induces integrin activation. This clasping/unclasping process is influenced by multiple cytoplasmic tail binding partners. Among them, talin appears to be a critical trigger of alpha(IIb)beta(3) activation, but other binding partners, which function as activators or suppressors, are likely to act as co-regulators of integrin activation.|Amino Acid Sequence[MESH]|Blood Platelets/*physiology[MESH]|Humans[MESH]|In Vitro Techniques[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Platelet Aggregation/physiology[MESH]|Platelet Glycoprotein GPIIb-IIIa Complex/*chemistry/*metabolism[MESH]|Protein Binding[MESH]|Protein Processing, Post-Translational[MESH]|Protein Structure, Tertiary[MESH]|Signal Transduction[MESH] |