Unique transmembrane domain interactions differentially modulate integrin αvβ3 and αIIbβ3 function.

ABSTRACT: Lateral transmembrane (TM) helix-helix interactions between single-span membrane proteins play an important role in the assembly and signaling of many cell-surface receptors. Often, these helices contain two highly conserved yet distinct interaction motifs, arranged such that the motifs cannot be engaged simultaneously. However, there is sparse experimental evidence that dual-engagement mechanisms play a role in biological signaling. Here, we investigate the function of the two conserved interaction motifs in the TM domain of the integrin β3-subunit. The first motif uses reciprocating "large-large-small" amino acid packing to mediate the interaction of the β3 and αIIb TM domains and maintain the inactive resting conformation of the platelet integrin αIIbβ3. The second motif, S-x₃

SUBMITTER: Litvinov RI 

PROVIDER: S-EPMC6589676 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature