Roles of N-linked glycosylation in SNS-Duf/Kirre mediated cell-cell adhesion

Abstract

To better understand SNS-Duf/Kirre mediated founder-fusion competent myoblast cell-cell recognition, we have addressed N-glycan requirements in SNS-Duf/Kirre mediated adhesion. Through site directed mutagenesis of N-glycosylation sites we have generated forms of SNS and Duf/Kirre lacking all N-glycans. Analysis of these mutants in S2 cell aggregation assays demonstrate a specific requirement for N-glycosylation of SNS in SNS-Duf/Kirre mediated aggregation, and for Duf/Kirre in Duf/Kirre-Duf/Kirre mediated aggregation. Since rescue experiments using SNS N-glycosylation mutants show only mild defects, it is apparent that, although the presence SNS is required for founder-fusion competent myoblast recognition, it is not the only molecule involved in proper execution of this process.