Your browser doesn't support javascript.
loading
Molecular structures of coat and coat-associated proteins: function follows form.
Brett, Tom J; Traub, Linton M.
Affiliation
  • Brett TJ; Department of Pathology and Immunology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
Curr Opin Cell Biol ; 18(4): 395-406, 2006 Aug.
Article in En | MEDLINE | ID: mdl-16806884
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.
Subject(s)
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Clathrin-Coated Vesicles Type of study: Risk_factors_studies Limits: Animals Language: En Journal: Curr Opin Cell Biol Year: 2006 Type: Article Affiliation country: United States
Search on Google
Collection: 01-internacional Database: MEDLINE Main subject: Proteins / Clathrin-Coated Vesicles Type of study: Risk_factors_studies Limits: Animals Language: En Journal: Curr Opin Cell Biol Year: 2006 Type: Article Affiliation country: United States