Rap-linked cAMP signaling Epac proteins: compartmentation, functioning and disease implications

Autor: Anne-Coline Laurent, Magali Breckler, Bertrand Crozatier, Frank Lezoualc'h, Eric Morel, Magali Berthouze
Přispěvatelé: Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Université Fédérale Toulouse Midi-Pyrénées, Université Paris-Sud - Paris 11 (UP11), Signalisation et physiopathologie cardiaque, Université Paris-Sud - Paris 11 (UP11)-IFR141-Institut National de la Santé et de la Recherche Médicale (INSERM), Simon, Marie Francoise
Rok vydání: 2010
Předmět:
Zdroj: Cell Signal
Cell Signal, 2011, 23 (8), pp.1257-66. ⟨10.1016/j.cellsig.2011.03.007⟩
ISSN: 1873-3913
DOI: 10.1016/j.cellsig.2011.03.007⟩
Popis: International audience; Epac proteins respond to the second messenger cyclic AMP (cAMP) and are activated by Gs coupled receptors. They act as specific guanine nucleotide exchange factors (GEFs) for the small G proteins, Rap1 and Rap2 of the Ras family. A plethora of studies using 8-pCPT-2'-O-Me-cAMP, an Epac agonist, has revealed the importance of these multi-domain proteins in the control of key cellular functions such as cell division, migration, growth and secretion. Epac and protein kinase A (PKA) may act independently but are often associated with the same biological process, in which they fulfill either synergistic or opposite effects. In addition, compelling evidence is now accumulating about the formation of molecular complexes in distinct cellular compartments that influence Epac signaling and cellular function. Epac is spatially and temporally regulated by scaffold protein and its effectors are interconnected with other signaling pathways. Pathophysiological changes in Epac signaling may underlie certain diseases.
Databáze: OpenAIRE