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Review
. 1993 Nov:127-128:309-19.
doi: 10.1007/978-1-4615-2600-1_28.

A-kinase anchoring proteins: a key to selective activation of cAMP-responsive events?

V M Coghlan  1 , S E Bergeson, L Langeberg, G Nilaver, J D Scott
Affiliations
Review

A-kinase anchoring proteins: a key to selective activation of cAMP-responsive events?

V M Coghlan et al. Mol Cell Biochem. 1993 Nov.

Abstract

The cAMP-dependent protein kinase (PKA) regulates a variety of diverse biochemical events through the phosphorylation of target proteins. Because PKA is a multifunctional enzyme with a broad substrate specificity, its compartmentalization may be a key regulatory event in controlling which particular target substrates are phosphorylated. In recent years it has been demonstrated that differential localization of the type II holoenzyme is directed through interaction of the regulatory subunit (RII) with a family of A-Kinase Anchoring Proteins (AKAPs). In this report, we review evidence for PKA compartmentalization and discuss the structural and functional properties of AKAPs.

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