Akt/PKB: one kinase, many modifications.
Biochem J
; 468(2): 203-14, 2015 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-25997832
ABSTRACT
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 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 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.
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Base de dados:
MEDLINE
Assunto principal:
Processamento de Proteína Pós-Traducional
/
Proteínas Proto-Oncogênicas c-akt
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article