Energy landscape differences among integrins establish the framework for understanding activation.

ABSTRACT: Why do integrins differ in basal activity, and how does affinity for soluble ligand correlate with cellular adhesiveness? We show that basal conformational equilibrium set points for integrin α₄β₁ are cell type specific and differ from integrin α₅β₁ when the two integrins are coexpressed on the same cell. Although α₄β₁ is easier to activate, its high-affinity state binds vascular cell adhesion molecule and fibronectin 100- to 1,000-fold more weakly than α₅β₁ binds fibronectin. Furthermore, the difference in affinity between the high- and low-affinity states is more compressed in α₄β₁ (600- to 800-fold) than in α₅β₁ (4,000- to 6,000-fold). α₄β_1<

SUBMITTER: Li J 

PROVIDER: S-EPMC5748972 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature