Mitochondrial and nuclear kinase complex role of MAPKs and MKPs in the cyclic AMPc mediated response

PODEROSO CECILIA; DUARTE ALEJANDRA; BRION LAURA; GOMEZ NATALIA; MORI SEQUEIROS GARCÍA M MERCEDES; PODESTÁ ERNESTO J; PAZ CRISTINA

San Miguel de Tucumán, Tucumán, Argentina

Congreso; XLV Annual Meeting of Argentine Society for Biochemistry and Molecular Biology (SAIB); 2009

Argentine Society for Biochemistry and Molecular Biology (SAIB)

Protein phosphorylation mediated by the concerted action of kinases and phosphatases regulates key biological events such as cell growth, differentiation and apoptosis. The simultaneous stimulation of different signal pathways to produce several cellular responses involves a finite number of kinases and phosphatases. Thus, the spatial and temporal control of these enzymes is crucial for the selectivity and effectiveness of phospho/dephosphorylation events. The regulation of MAP kinases (MAPKs) and MAP kinase phosphatases (MKPs), which provide a negative feedback mechanism for MAPK activity, explains how this control is achieved. Phosphorylation induced by a specific stimulus promotes conformational changes, creates docking sites and causes intracellular relocation of proteins that finally results in the activation of a particular set of MAPKs in a specific compartment. The same stimulus also induces MKPs of different induction kinetics and subcellular localization. Thus, these coordinated events and the existence of a complex containing a specific substrate with kinases, phosphatases, docking and scaffolding proteins leads to the compartment-specific regulation of MAPKs to produce the right response in the right place. Here, the participation of nuclear and mitochondrial kinases and phosphatases complex in the induction and activation of key steroigenic proteins will be presented.