N. Kahner, Bryan Kato, Hisashi Banno, Asoka Ginsberg, Mark H. J. Shattil, Sanford Ye, Feng Model of agonist-induced αIIbβ3 activation. <p>(<b>A</b>) Stimulation of a platelet agonist receptor (e.g., PAR1) by an agonist leads to the activation of Rap1, resulting in targeting of its effector, RIAM, to the plasma membrane. (<b>B</b>) Cell stimulation also releases talin from its auto-inhibitory state, resulting in separation of the THD from the talin rod domain and recruitment of talin to the membrane-bound Rap1/RIAM complex. (<b>C</b>) Membrane-bound talin is recruited to αIIbβ3 by interaction of the THD with membrane-distal residues in the β3 cytoplasmic domain. (<b>D</b>) Further interactions of the THD with membrane-proximal β3 tail residues and membrane phospholipids leads to separation of the αIIb and β3 tail and transmembrane domains, triggering propagated changes in the extracellular domains leading to high-affinity binding of adhesive ligands, such as fibrinogen. While kindlins, like talin, can interact with the β3 cytoplasmic tail, they can also bind to other proteins <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0034056#pone.0034056-Moser3" target="_blank">[20]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0034056#pone.0034056-Malinin1" target="_blank">[42]</a>, and the molecular basis of their integrin co-activating function remains unclear. This working model is based on published studies summarized in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0034056#pone.0034056-Shattil1" target="_blank">[2]</a>.</p> agonist-induced 2012-03-23
    https://plos.figshare.com/articles/figure/_Model_of_agonist_induced_945_IIb_946_3_activation_/333735
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