Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats Journal Article

   

Authors:	Lee, C.; Goldberg, J.
Article Title:	Structure of coatomer cage proteins and the relationship among COPI, COPII, and clathrin vesicle coats
Abstract:	COPI-coated vesicles form at the Golgi apparatus from two cytosolic components, ARF G protein and coatomer, a heptameric complex that can polymerize into a cage to deform the membrane into a bud. Although coatomer shares a common evolutionary origin with COPII and clathrin vesicle coat proteins, the architectural relationship among the three cages is unclear. Strikingly, the αβ'-COP core of coatomer crystallizes as a triskelion in which three copies of a β'-COP β-propeller domain converge through their axial ends. We infer that the trimer constitutes the vertex of the COPI cage. Our model proposes that the COPI cage is intermediate in design between COPII and clathrin: COPI shares with clathrin an arrangement of three curved α-solenoid legs radiating from a common center, and COPI shares with COPII highly similar vertex interactions involving the axial ends of β-propeller domains. © 2010 Elsevier Inc.
Keywords:	protein domain; proteins; animals; protein interaction; amino acid sequence; molecular sequence data; sequence alignment; cellbio; crystal structure; models, molecular; crystallography, x-ray; protein structure, tertiary; cattle; protein structure; structure analysis; clathrin; coat protein complex i; coat protein complex ii; coatomer protein; coated vesicle; cop-coated vesicles; solenoidea; triskelion
Journal Title:	Cell
Volume:	142
Issue:	1
ISSN:	0092-8674
Publisher:	Cell Press
Date Published:	2010-07-09
Start Page:	123
End Page:	132
Language:	English
DOI:	10.1016/j.cell.2010.05.030
PUBMED:	20579721
PROVIDER:	scopus
PMCID:	PMC2943847
DOI/URL:	http://www.scopus.com/inward/record.url?eid=2-s2.0-77954310096&partnerID=40&md5=3ac48933da037ad29ef860d859d8bfb1
Notes:	--- - "Cited By (since 1996): 7" - "Export Date: 20 April 2011" - "CODEN: CELLB" - "Source: Scopus"

https://synapse.mskcc.org/synapse/works/has_related_data_chk/4472