title: Broad yet high substrate specificity: the challenge of AAA+ proteins.
abstract: AAA+ proteins remodel target substrates in an ATP-dependent manner, an activity that is of central importance for a plethora of cellular processes. While sharing a similar hexameric structure AAA+ proteins must exhibit differences in substrate recognition to fulfil their diverse biological functions. Here we describe strategies of AAA+ proteins to ensure substrate specificity. AAA domains can directly mediate substrate recognition, however, in general extra domains, added to the core AAA domain, control substrate interaction. Such extra domains may either directly recognize substrates or serve as a platform for adaptor proteins, which transfer bound substrates to their AAA+ partner proteins. The positioning of adaptor proteins in substrate recognition can enable them to control the activity of their partner proteins by coupling AAA+ protein activation to substrate availability.
authors.affiliation: Zentrum für Molekulare Biologie Heidelberg, Universität Heidelberg, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. a.mogk@zmbh.uni-heidelberg.de
authors.forename: Axel
authors.initials: A
authors.lastname: Mogk
authors.forename: David
authors.initials: D
authors.lastname: Dougan
authors.forename: Jimena
authors.initials: J
authors.lastname: Weibezahn
authors.forename: Christian
authors.initials: C
authors.lastname: Schlieker
authors.forename: Kursad
authors.initials: K
authors.lastname: Turgay
authors.forename: Bernd
authors.initials: B
authors.lastname: Bukau
mesh_terms: D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism; D004789:Enzyme Activation; D043583:Nucleoside-Triphosphatase / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D033942:Adaptor Proteins, Vesicular Transport; D043583:Nucleoside-Triphosphatase