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

ABSTRACT: Membrane tension plays an inhibitory role in clathrin-mediated endocytosis (CME) by impeding the transition of flat plasma membrane to hemispherical clathrin-coated structures (CCSs). Membrane tension also impedes the transition of hemispherical domes to omega-shaped CCSs. However, CME is not completely halted in cells under high tension conditions. Here we find that epsin, a membrane bending protein which inserts its N-terminus H₀ helix into lipid bilayer, supports flat-to-dome transition of a CCS and stabilizes its curvature at high tension. This discovery is supported by molecular dynamic simulation of the epsin N-terminal homology (ENTH) domain that becomes more structured when embedded in a lipid bilayer. In addition, epsin has an intrinsically disordered protein (IDP) C-te

SUBMITTER: Joseph JG 

PROVIDER: S-EPMC7722716 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature