A Structural Mechanism of Integrin αIIbβ3 “Inside-Out” Activation as Regulated by Its Cytoplasmic Face

By O. Vinogradova, Algirdas Velyvis, Asta Velyviene, Bin Hu, T. Haas, E. Plow, J. Qin. 2002

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Structural basis of integrin activation by talin. (2007, background): “(NMR) spectroscopic evidence has suggested an interaction between talin F3 and the membrane-proximal (MP) btail region (Ulmer et al., 2003; Vinogradova et al., 2002) that is important for activation (Hughes et al., 1995; Ulmer et al., 2003).”
Integrin structure, activation, and interactions. (2011, background): “A study of isolated mixed peptides found two distinct structures of the ab complex (Weljie et al. 2002), both significantly different from the most detailed published structure of the ab tail complex (Vinogradova et al. 2002).”
Structural basis of integrin regulation and signaling. (2007, background): “NMR studies of the integrin cytoplasmic tails suggest that their association is weak, with significant differences between published structures of associated cytoplasmic domains (85, 86) or with undetectable association between α and β subunit cytoplasmic domains (87, 88).”
Activation of a vinculin‐binding site in the talin rod involves rearrangement of a five‐helix bundle (2004, background): “…(Brown et al, 2002) and mouse (Monkley et al, 2000) confirm that talin is essential for integrin-mediated developmental events and (v) talin activates integrins (Tadokoro et al, 2003) by disrupting the interaction between the ab-subunit cytodomains (Vinogradova et al, 2002; Kim et al, 2003).”