CONICET | Buscador de Institutos y Recursos Humanos

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 thus considered a key signaling molecule in higher eukaryotes. Deregulation of Akt signaling is associated with a variety of human diseases, revealing Akt-‐dependent pathways as an attractive target for therapeutic intervention. Since its discovery at the early 90?s, a large body of work has focus on Akt phosphorylation on two residues, threonine 308 and serine 473, and modification on these two sites has been established as equivalent to Akt activation. More recently, Akt has been identified as a substrate for many different post-‐translational 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 signaling molecule. In this review we will provide an overview of these different post-‐ translational modifications identified for Akt, focusing in their consequences on this kinase activity.