Receptor Heterodimerization Modulates Endocytosis through Collaborative and Competitive Mechanisms.

ABSTRACT: Recruitment of receptors into clathrin-coated structures is essential to signal transduction and nutrient uptake. Among the many receptors involved in these processes, a significant fraction forms dimers. Dimerization of identical partners has generally been thought to promote receptor recruitment for uptake because of increased affinity of the dimer for the endocytic machinery. But what happens when receptors with substantially different affinities for the endocytic machinery come together to form a heterodimer? Evidence from diverse receptor classes, including G-protein-coupled receptors and receptor tyrosine kinases, suggests that heterodimerization with a strongly recruited receptor can drive significant recruitment of a receptor that lacks direct interactions with the endocytic machin

SUBMITTER: Zhao C 

PROVIDER: S-EPMC6712433 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature