1H0A

Epsin ENTH bound to Ins(1,4,5)P3

Summary for 1H0A

• Entry DOI: 10.2210/pdb1h0a/pdb
• Related: 1EDU 1EYH
• Descriptor: EPSIN, 1,4-DIETHYLENE DIOXIDE, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: endocytosis, epsin, enth, clathrin, triskelion, coated vesicles, alpha-alpha superhelix, ins(1, 4, 5)p3
• Biological source: RATTUS NORVEGICUS (RAT)
• Cellular location: Cytoplasm: O88339
• Total number of polymer chains: 1
• Total formula weight: 19276.63

Authors

Ford, M.G.J.,McMahon, H.T.,Evans, P.R. (deposition date: 2002-06-12, release date: 2002-10-03, Last modification date: 2023-12-13)

Primary citation

Ford, M.G.J.,Mills, I.,Peter, B.,Vallis, Y.,Praefcke, G.,Evans, P.R.,Mcmahon, H.T.
Curvature of Clathrin-Coated Pits Driven by Epsin
Nature, 419:361-, 2002

PubMed Abstract: 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 alpha-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.

PubMed: 12353027
DOI: 10.1038/NATURE01020

Experimental method

X-RAY DIFFRACTION (1.7 Å)