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AKAP79 and the evolution of the AKAP model
Author(s) -
Dodge Kimberley,
Scott John D
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01671-9
Subject(s) - compartmentalization (fire protection) , microbiology and biotechnology , scaffold protein , upstream (networking) , domain (mathematical analysis) , protein kinase a , protein kinase domain , enzyme , kinase , computational biology , chemistry , biology , biophysics , biochemistry , signal transduction , computer science , computer network , mathematical analysis , mathematics , mutant , gene
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.