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PMID: 16806884 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

Molecular structures of coat and coat-associated proteins: function follows form.

Current opinion in cell biology ·Vol. 18 ·No. 4 ·2006-08-00 ·Pages 395-406

Brett TJ, Traub LM

Abstract

Endocytic clathrin-coated vesicles arise through the deformation of a small region of plasma membrane encapsulated by a cytosol-oriented clathrin lattice. The coat assembles from soluble protomers in a rapid and highly cooperative process, and invagination is tightly linked to the selective enrichment of cargo molecules within the nascent bud. Recent structural and functional studies demonstrate that coat assembly, membrane deformation, local actin dynamics and the final scission event are intricately coupled, and begin to reveal how key multifunctional, modular proteins are responsible for this linkage. An emerging mechanistic theme is how sequential engagement of common interaction surfaces or network hubs can evict prior binding partners from the assembly zone to ensure vectorial progression of the coat assembly process.

MeSH Terms
Animals Cell Membrane/physiology Clathrin-Coated Vesicles/chemistry,physiology Models, Biological Proteins/chemistry,physiology
Chemicals
Proteins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Brett Tom J
Department of Pathology and Immunology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
Traub Linton M
Article Info
Journal
Current opinion in cell biology
Abbr.
Curr Opin Cell Biol
ISSN
0955-0674
Published
2006-08-00
Epub
2006-00-27
Pages
395-406
Language
English
Region
England
NLM ID
8913428
Subset
IM
Grants
NIGMS NIH HHS · GM62414-04 · United States
NIDDK NIH HHS · R01 DK53249 · United States
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