Enhanced receptor-clathrin interactions induced by N-glycan-mediated membrane micropatterning.

ABSTRACT: Glycan-protein interactions are emerging as important modulators of membrane protein organization and dynamics, regulating multiple cellular functions. In particular, it has been postulated that glycan-mediated interactions regulate surface residence time of glycoproteins and endocytosis. How this precisely occurs is poorly understood. Here we applied single-molecule-based approaches to directly visualize the impact of glycan-based interactions on the spatiotemporal organization and interaction with clathrin of the glycosylated pathogen recognition receptor dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN). We find that cell surface glycan-mediated interactions do not influence the nanoscale lateral organization of DC-SIGN but restrict the mobility of

SUBMITTER: Torreno-Pina JA 

PROVIDER: S-EPMC4121791 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature