The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling.

ABSTRACT: Heterodimeric integrin adhesion receptors regulate cell migration, survival and differentiation in metazoa by communicating signals bi-directionally across the plasma membrane. Protein engineering and mutagenesis studies have suggested that the dissociation of a complex formed by the single-pass transmembrane (TM) segments of the alpha and beta subunits is central to these signalling events. Here, we report the structure of the integrin alphaIIbbeta3 TM complex, structure-based site-directed mutagenesis and lipid embedding estimates to reveal the structural event that underlies the transition from associated to dissociated states, that is, TM signalling. The complex is stabilized by glycine-packing mediated TM helix crossing within the extracellular membrane leaflet, and by unique hydropho

SUBMITTER: Lau TL 

PROVIDER: S-EPMC2683045 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature