Tailoring cAMP-signalling responses through isoform multiplicity

Trends Biochem Sci. 1997 Jun;22(6):217-24. doi: 10.1016/s0968-0004(97)01050-5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • 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*

Substances

  • Isoenzymes
  • Cyclic AMP
  • Cyclic AMP-Dependent Protein Kinases
  • 3',5'-Cyclic-AMP Phosphodiesterases
  • GTP-Binding Proteins
  • Adenylyl Cyclases
  • Cyclic GMP
  • Calcium