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Curvature of clathrin-coated pits driven by epsin
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Journal Article
Curvature of clathrin-coated pits driven by epsin
2002
Overview
Clathrin-mediated endocytosis involves cargo selection and membrane budding into vesicles with the aid of a protein coat. Formation of invaginated pits on the plasma membrane and subsequent budding of vesicles is an energetically demanding process that involves the cooperation of clathrin with many different proteins. Here we investigate the role of the brain-enriched protein epsin 1 in this process. Epsin is targeted to areas of endocytosis by binding the membrane lipid phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P
2
). We show here that epsin 1 directly modifies membrane curvature on binding to PtdIns(4,5)P
2
in conjunction with clathrin polymerization. We have discovered that formation of an amphipathic α-helix in epsin is coupled to PtdIns(4,5)P
2
binding. Mutation of residues on the hydrophobic region of this helix abolishes the ability to curve membranes. We propose that this helix is inserted into one leaflet of the lipid bilayer, inducing curvature. On lipid monolayers epsin alone is sufficient to facilitate the formation of clathrin-coated invaginations.
Publisher
Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
Subject
Adaptor Proteins, Vesicular Transport
/ Animals
/ Biological and medical sciences
/ Brain
/ Carrier Proteins - chemistry
/ Carrier Proteins - metabolism
/ Cell membranes. Ionic channels. Membrane pores
/ Cell structures and functions
/ Coated Pits, Cell-Membrane - chemistry
/ Coated Pits, Cell-Membrane - metabolism
/ Coated Pits, Cell-Membrane - ultrastructure
/ Fundamental and applied biological sciences. Psychology
/ Humanities and Social Sciences
/ Humans
/ Inositol 1,4,5-Trisphosphate - metabolism
/ Membrane Proteins - metabolism
/ Molecular and cellular biology
/ Mutation
/ Phosphatidylinositol 4,5-Diphosphate - metabolism
/ Rats
/ Science
