5AHV

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

5AHV の概要

• エントリーDOI: 10.2210/pdb5ahv/pdb
• EMDBエントリー: 2896
• 分子名称: ENTH DOMAIN OF EPSIN ENT1, ANTH DOMAIN OF ENDOCYTIC ADAPTOR SLA2 (2 entities in total)
• 機能のキーワード: clathrin-binding protein, clathrin binding protein, epsin, hip1r, enth, clathrin adaptors, endocytosis
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm: Q12518; Cell membrane ; Single-pass membrane protein : P33338
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48706.43

構造登録者

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. (登録日: 2015-02-10, 公開日: 2015-05-06, 最終更新日: 2024-07-10)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (13.6 Å)