Adhesion-induced unclasping of cytoplasmic tails of integrin alpha(IIb)beta3.

Biochemistry
Nataly P PodolnikovaTatiana P Ugarova

Abstract

Integrin alpha(IIb)beta(3) plays a pivotal role in hemostasis and thrombosis by mediating adhesive interactions of platelets. Binding of alpha(IIb)beta(3) to its physiological ligands, immobilized fibrinogen and fibrin, induces outside-in signaling in platelets, leading to their adhesion and spreading even without prior stimulation by agonists. Implicit in these phenomena is a requirement for the linkage between integrins' cytoplasmic tails and intracellular proteins. However, the nature of the initiating signal has not been established. In this study, we examined whether binding of alpha(IIb)beta(3) to immobilized fibrin(ogen), per se, triggers interaction of the integrin with cytoplasmic proteins. Using the integrin-binding skelemin fragment as a marker of exposure of residues involved in the clasp between alpha(IIb) and beta(3) cytoplasmic tails, we showed that its binding site in the membrane-proximal beta(3) 715-730 segment is cryptic and becomes exposed as a result of binding of isolated alpha(IIb)beta(3) to immobilized ligands. Furthermore, the skelemin-like protein present in platelets and CHO cells does not associate with alpha(IIb)beta(3) in resting platelets or suspended alpha(IIb)beta(3)-expressing CHO cells but is ...Continue Reading

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Citations

Sep 17, 2014·Biochemistry·Vitaliy GorbatyukOlga Vinogradova
Jan 1, 2013·Biochemistry·Xinlei LiThomas A Haas
Jul 18, 2019·Physiological Reviews·Michael BachmannBernhard Wehrle-Haller
Feb 13, 2016·The Journal of Biological Chemistry·Rustem I LitvinovJoel S Bennett
May 4, 2021·Frontiers in Cell and Developmental Biology·Wolfgang M J ObermannJohannes A Eble

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