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TitleAn organized co-assembly of clathrin adaptors is essential for endocytosis.
Journal, issue, pagesDev Cell, Vol. 33, Issue 2, Page 150-162, Year 2015
Publish dateApr 20, 2015
AuthorsMichal Skruzny / Ambroise Desfosses / Simone Prinz / Svetlana O Dodonova / Anna Gieras / Charlotte Uetrecht / Arjen J Jakobi / Marc Abella / Wim J H Hagen / Joachim Schulz / Rob Meijers / Vladimir Rybin / John A G Briggs / Carsten Sachse / Marko Kaksonen /
PubMed AbstractClathrin-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 ...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.
External linksDev Cell / PubMed:25898165
MethodsEM (single particle)
Resolution13.6 - 18.3 Å
Structure data

2896

5ahv

EMDB-2896, PDB-5ahv:
Cryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranes
Method: EM (single particle) / Resolution: 13.6 Å

EMDB-2897:
Cryo-EM structure of helical ANTH and ENTH tubules on PI(4,5)P2-containing membranes
Method: EM (single particle) / Resolution: 18.3 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCLATHRIN-BINDING PROTEIN / CLATHRIN BINDING PROTEIN / EPSIN / HIP1R / ENTH / CLATHRIN ADAPTORS / ENDOCYTOSIS

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