Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 35, Issue -, Pages 931-937Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0350931
Keywords
A-kinase-anchoring protein (AKAP); cAMP; compartmentalization; extracellular-signal-regulated kinase (ERK); phosphodiesterase (PDE); protein kinase A (PKA)
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Ligand-induced changes in cAMP concentration vary in duration, amplitude and extension into the cell. cAMP microdomains are shaped by adenylate cyclases that form cAMP as well as PDEs (phosphodiesterases) that degrade cAMP. Various extracellular signals converge on the cAMP/PKA (protein kinase A) pathway through ligand binding to GPCRs (G-protein-coupled receptors) and the cAMP/PKA pathway is therefore tightly regulated on several levels to maintain specificity in the multitude of signal inputs. AKAPs (A-kinase-anchoring proteins) target PKA to specific substrates and distinct subcellular compartments, providing spatial and temporal specificity for mediation of biological effects channelled through the cAMP/PKA pathway. AKAPs also serve as scaffolding proteins that assemble PKA together with signal terminators such as phosphoprotein phosphatases and cAMP-specific PDEs as well as components of other signalling pathways into multiprotein signalling complexes.
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