title: AKAP79 and the evolution of the AKAP model.
abstract: A molecular explanation for the specificity of the cAMP-dependent protein kinase (PKA) can be provided by its compartmentalization through association with A-kinase-anchoring proteins (AKAPs). Structural and functional studies have led to the development of an anchoring model proposing that AKAPs contain a common PKA binding domain and a unique subcellular targeting domain. The discovery that AKAPs can bind other signaling enzymes led to the addition of a third property, that of scaffolding molecule. Recent research has now expanded the role of AKAPs to members of multiunit complexes containing both upstream activators and downstream targets.
authors.affiliation: Howard Hughes Medical Institute, Vollum Institute, 3181 S.W. Sam Jackson Park Road, 97201-3098, Portland, OR, USA.
authors.forename: K
authors.initials: K
authors.lastname: Dodge
authors.forename: J D
authors.initials: JD
authors.lastname: Scott
mesh_terms: D054758:A Kinase Anchor Proteins; D048868:Adaptor Proteins, Signal Transducing; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics / Q000502:physiology*; D002462:Cell Membrane / Q000502:physiology; D006801:Humans; D008959:Models, Neurological; D009474:Neurons / Q000502:physiology*; D015398:Signal Transduction
chemical_list: D054758:A Kinase Anchor Proteins; C487775:AKAP5 protein, human; D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins