The assembly of diverse immune receptors is focused on a polar membrane-embedded interaction site

Abstract

The majority of receptors responsible for activation of distinct cell types within the immune system assemble with dimeric signaling modules through interaction of a basic transmembrane residue with a pair of acidic residues of the signaling dimer. Because assembly of other membrane proteins requires specific interactions along extended stretches of transmembrane helices, we examined how transmembrane sequences flanking the polar interaction site contribute to assembly for three receptors that associate with different signaling modules - the natural killer cell receptors KIR and NKG2D and the Fc receptor for IgA, FcaRI. The KIR and NKG2D receptors assembled with the DAP12 and DAP10 dimers, r..