Artículos de revistas
Akt/PKB: one kinase, many modifications
Fecha
2015-06Registro en:
Risso, Guillermo; Blaustein Kappelmacher, Matias; Pozzi, María Berta; Mammi, Pablo Andrés; Srebrow, Anabella; Akt/PKB: one kinase, many modifications; Portland Press; Biochemical Journal; 468; 2; 6-2015; 203-214
0264-6021
CONICET Digital
CONICET
Autor
Risso, Guillermo
Blaustein Kappelmacher, Matias
Pozzi, María Berta
Mammi, Pablo Andrés
Srebrow, Anabella
Resumen
Akt/PKB, a serine/threonine kinase member of the AGC family of proteins, is involved in the regulation of a plethora of cellular processes triggered by a wide diversity of extracellular signals and is thus considered a key signalling molecule in higher eukaryotes. Deregulation of Akt signalling is associated with a variety of human diseases, revealing Akt-dependent pathways as an attractive target for therapeutic intervention. Since its discovery in the early 1990s, a large body of work has focused on Akt phosphorylation of two residues, Thr308 and Ser473, and modification of these two sites has been established as being equivalent to Akt activation. More recently, Akt has been identified as a substrate for many different posttranslational modifications, including not only phosphorylation of other residues, but also acetylation, glycosylation, oxidation, ubiquitination and SUMOylation. These modifications could provide additional regulatory steps for fine-tuning Akt function, Akt trafficking within the cell and/or for determining the substrate specificity of this signalling molecule. In the present review, we provide an overview of these different post-translational modifications identified for Akt, focusing on their consequences for this kinase activity.