5AHV

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

Summary for 5AHV

• Entry DOI: 10.2210/pdb5ahv/pdb
• EMDB information: 2896
• Descriptor: ENTH DOMAIN OF EPSIN ENT1, ANTH DOMAIN OF ENDOCYTIC ADAPTOR SLA2 (2 entities in total)
• Functional Keywords: clathrin-binding protein, clathrin binding protein, epsin, hip1r, enth, clathrin adaptors, endocytosis
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm: Q12518; Cell membrane ; Single-pass membrane protein : P33338
• Total number of polymer chains: 2
• Total formula weight: 48706.43

Authors

Skruzny, M.,Desfosses, A.,Prinz, S.,Dodonova, S.O.,Gieras, A.,Uetrecht, C.,Jakobi, A.J.,Abella, M.,Hagen, W.J.H.,Schulz, J.,Meijers, R.,Rybin, V.,Briggs, J.A.G.,Sachse, C.,Kaksonen, M. (deposition date: 2015-02-10, release date: 2015-05-06, Last modification date: 2024-07-10)

Primary citation

Skruzny, M.,Desfosses, A.,Prinz, S.,Dodonova, S.O.,Gieras, A.,Uetrecht, C.,Jakobi, A.J.,Abella, M.,Hagen, W.J.H.,Schulz, J.,Meijers, R.,Rybin, V.,Briggs, J.A.G.,Sachse, C.,Kaksonen, M.
An Organized Co-Assembly of Clathrin Adaptors is Essential for Endocytosis.
Dev.Cell, 33:150-, 2015

PubMed Abstract: 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.

PubMed: 25898165
DOI: 10.1016/J.DEVCEL.2015.02.023

Experimental method

ELECTRON MICROSCOPY (13.6 Å)