Complimentary action of structured and unstructured domains of epsin supports clathrin-mediated endocytosis at high tension

Abstract

Using imaging and molecular dynamics simulations, Joseph et al characterize the tension-responsive recruitment of the membrane bending protein epsin and its stabilization of clathrin-coated structures (CCSs) to form clathrin-coated pits. They find epsin’s ENTH- and unstructured IDP domains play complementary roles in CCS maturation under high tension.