Epac proteins: multi-purpose cAMP targets

Trends Biochem Sci. 2006 Dec;31(12):680-6. doi: 10.1016/j.tibs.2006.10.002. Epub 2006 Nov 2.


Epac1 and Epac2 are cAMP-dependent guanine-nucleotide-exchange factors for the small GTPases Rap1 and Rap2, and are known to be important mediators of cAMP signaling. The recent determination of the crystal structure of Epac2 has indicated a mechanism for the activation of the multi-domain Epac proteins. In addition, these proteins have been implicated in various cellular processes such as integrin-mediated cell adhesion and cell-cell junction formation, the control of insulin secretion and neurotransmitter release. In most of these processes, cAMP signaling through protein kinase A (PKA) is also involved, stressing the interconnectivity between Epac- and PKA-mediated signaling.

Publication types

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

MeSH terms

  • Animals
  • Cell Adhesion
  • Cyclic AMP / chemistry*
  • Cyclic AMP / metabolism
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Glucose / metabolism
  • Guanine Nucleotide Exchange Factors / physiology*
  • Humans
  • Integrins / metabolism
  • Leukemia Inhibitory Factor / metabolism
  • Models, Biological
  • Models, Chemical
  • Protein Conformation
  • Protein Structure, Tertiary
  • Signal Transduction


  • Guanine Nucleotide Exchange Factors
  • Integrins
  • Leukemia Inhibitory Factor
  • RAPGEF3 protein, human
  • RAPGEF4 protein, human
  • Cyclic AMP
  • Cyclic AMP-Dependent Protein Kinases
  • Glucose