Tailoring cAMP-signalling responses through isoform multiplicity

Multiple forms of cAMP phosphodiesterases (PDE), adenylate cyclase and protein kinase A (PKA) allow cells to tailor the responsiveness of the cAMP-signalling system and to allow for its dynamic adjustment. Multiple forms of these enzymes confer spatial and temporal characteristics on cAMP signalling...

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Bibliographic Details
Published in:Trends in Biochemical Sciences 1997-06, Vol.22 (6), p.217-224
Main Authors: Houslay, Miles D., Milligan, Graeme
Format: Article
Language:English
Subjects:
3',5'-Cyclic-AMP Phosphodiesterases - chemistry
3',5'-Cyclic-AMP Phosphodiesterases - metabolism
Adenylyl Cyclases - chemistry
Adenylyl Cyclases - metabolism
Animals
Calcium - pharmacology
Cyclic AMP - metabolism
Cyclic AMP-Dependent Protein Kinases - chemistry
Cyclic AMP-Dependent Protein Kinases - metabolism
Cyclic GMP - metabolism
GTP-Binding Proteins - metabolism
GTP-Binding Proteins - physiology
Isoenzymes - chemistry
Isoenzymes - metabolism
Models, Molecular
Phosphorylation
Signal Transduction - physiology
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Summary:Multiple forms of cAMP phosphodiesterases (PDE), adenylate cyclase and protein kinase A (PKA) allow cells to tailor the responsiveness of the cAMP-signalling system and to allow for its dynamic adjustment. Multiple forms of these enzymes confer spatial and temporal characteristics on cAMP signalling so as to affect compartmentalised responses within a single cell type. The ability to breach the PKA activation threshold can depend upon either or both the activation of adenylate cyclase and inhibition of specific PDE isoforms.
ISSN:0968-0004
1362-4326
DOI:10.1016/S0968-0004(97)01050-5