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Cryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranes
Structural highlights
FunctionENT1_YEAST Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. Negatively regulated via phosphorylation.[1] [2] [3] Publication Abstract from PubMedClathrin-mediated endocytosis, the main trafficking route from the plasma membrane to the cytoplasm, is critical to many fundamental cellular processes. Clathrin, coupled to the membrane by adaptor proteins, is thought to play a major structural role in endocytosis by self-assembling into a cage-like lattice around the forming vesicle. Although clathrin adaptors are essential for endocytosis, little is known about their structural role in this process. Here we show that the membrane-binding domains of two conserved clathrin adaptors, Sla2 and Ent1, co-assemble in a PI(4,5)P2-dependent manner to form organized lattices on membranes. We determined the structure of the co-assembled lattice by electron cryo-microscopy and designed mutations that specifically impair the lattice formation in vitro. We show that these mutations block endocytosis in vivo. We suggest that clathrin adaptors not only link the polymerized clathrin to the membrane but also form an oligomeric structure, which is essential for membrane remodeling during endocytosis. An Organized Co-assembly of Clathrin Adaptors Is Essential for Endocytosis.,Skruzny M, Desfosses A, Prinz S, Dodonova SO, Gieras A, Uetrecht C, Jakobi AJ, Abella M, Hagen WJ, Schulz J, Meijers R, Rybin V, Briggs JA, Sachse C, Kaksonen M Dev Cell. 2015 Apr 20;33(2):150-62. doi: 10.1016/j.devcel.2015.02.023. PMID:25898165[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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