Epac proteins: multi-purpose cAMP targets.
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.
Bos
Johannes L
JL
Department of Physiological Chemistry and Centre for Biomedical Genetics, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands. j.l.bos@med.uu.nl
D000818:Animals; D002448:Cell Adhesion; D000242:Cyclic AMP / Q000737:chemistry* / Q000378:metabolism; D017868:Cyclic AMP-Dependent Protein Kinases / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D020662:Guanine Nucleotide Exchange Factors / Q000502:physiology*; D006801:Humans; D016023:Integrins / Q000378:metabolism; D053605:Leukemia Inhibitory Factor / Q000378:metabolism; D008954:Models, Biological; D008956:Models, Chemical; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
D020662:Guanine Nucleotide Exchange Factors; D016023:Integrins; D053605:Leukemia Inhibitory Factor; C116122:RAPGEF3 protein, human; C442864:RAPGEF4 protein, human; D000242:Cyclic AMP; D017868:Cyclic AMP-Dependent Protein Kinases; D005947:Glucose