5ahv

Cryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranesCryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranes

5ahv, resolution 13.60Å Show:Asymmetric Unit Biological Assembly Structural highlights 5ahv is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ENT1_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. [SLA2_YEAST] Required for cellular morphogenesis and polarization of the cortical cytoskeleton. It might act in concert with proteins such as CDC42 and CDC43 to limit the region of cortical patch formation to the cortex of the bud. Required for the accumulation and/or maintenance of plasma membrane H(+)-ATPase on the cell surface. Publication Abstract from PubMed Clathrin-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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Epsin