Document Detail


The clathrin adaptor complexes as a paradigm for membrane-associated allostery.
MedLine Citation:
PMID:  23424177     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The clathrin-associated adaptor protein (AP) complexes AP-1 and AP-2 are two members of a family of heterotetrameric assemblies that connect transmembrane protein cargo to vesicular coats. Cargo binding by AP-1 is activated by the small GTPase Arf1, while AP-2 is activated by the phosphoinositide PI(4,5)P₂. The structures of both AP-1 and AP-2 have been determined in their locked and unlocked conformations. The structures show how different activators use different mechanisms to trigger similar large scale conformational rearrangements. The details of these mechanisms show how membrane docking and allosteric activation of AP complexes are intimately connected.
Authors:
Bertram J Canagarajah; Xuefeng Ren; Juan S Bonifacino; James H Hurley
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Intramural; Review     Date:  2013-03-18
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  22     ISSN:  1469-896X     ISO Abbreviation:  Protein Sci.     Publication Date:  2013 May 
Date Detail:
Created Date:  2013-04-26     Completed Date:  2013-11-06     Revised Date:  2014-05-07    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  517-29     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 The Protein Society.
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MeSH Terms
Descriptor/Qualifier:
ADP-Ribosylation Factor 1 / metabolism
Adaptor Protein Complex 1 / analysis,  metabolism*
Adaptor Protein Complex 2 / analysis,  metabolism*
Allosteric Regulation
Animals
Binding Sites
Coated Vesicles / chemistry,  metabolism*
Humans
Models, Molecular
Phosphatidylinositols / metabolism
Protein Conformation
Chemical
Reg. No./Substance:
0/Adaptor Protein Complex 1; 0/Adaptor Protein Complex 2; 0/Phosphatidylinositols; EC 3.6.5.2/ADP-Ribosylation Factor 1
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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