Receptor heterodimerization modulates endocytic recruitment through collaborative and competitive mechanisms (Biophysical Journal)

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 form dimers. Dimerization of identical partners has generally been thought to promote receptor recruitment for uptake owing to 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 machinery.