Interactions of platelet integrin alphaIIb and beta3 transmembrane domains in mammalian cell membranes and their role in integrin activation.

ABSTRACT: Clustering and occupancy of platelet integrin alpha(IIb)beta(3) (GPIIb-IIIa) generate biologically important signals: conversely, intracellular signals increase the integrins' affinity, leading to integrin activation; both forms of integrin signaling play important roles in hemostasis and thrombosis. Indirect evidence implicates interactions between integrin alpha and beta transmembrane domains (TMDs) and cytoplasmic domains in integrin signaling; however, efforts to directly identify these associations have met with varying and controversial results. In this study, we develop mini-integrin affinity capture and use it in combination with nuclear magnetic resonance spectroscopy to show preferential heterodimeric association of integrin alpha(IIb)beta(3) TMD tails via specific TMD interactio

SUBMITTER: Kim C 

PROVIDER: S-EPMC2680374 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature