title: The clathrin adaptor complexes as a paradigm for membrane-associated allostery.
abstract: 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: Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA.
authors: Bertram J
authors: BJ
authors: Canagarajah
authors: Xuefeng
authors: X
authors: Ren
authors: Juan S
authors: JS
authors: Bonifacino
authors: James H
authors: JH
authors: Hurley
mesh_terms: D020823:ADP-Ribosylation Factor 1 / Q000378:metabolism; D033961:Adaptor Protein Complex 1 / Q000032:analysis / Q000378:metabolism*; D033962:Adaptor Protein Complex 2 / Q000032:analysis / Q000378:metabolism*; D000494:Allosteric Regulation; D000818:Animals; D001665:Binding Sites; D018699:Coated Vesicles / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D010716:Phosphatidylinositols / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D033961:Adaptor Protein Complex 1; D033962:Adaptor Protein Complex 2; D010716:Phosphatidylinositols; D020823:ADP-Ribosylation Factor 1