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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June 2015
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Review Article|
May 22 2015
Akt/PKB: one kinase, many modifications
Guillermo Risso;
Guillermo Risso
*Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE, UBA-CONICET), Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires (C1428EHA), Argentina
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Matías Blaustein;
Matías Blaustein
1
*Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE, UBA-CONICET), Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires (C1428EHA), Argentina
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Berta Pozzi;
Berta Pozzi
1
*Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE, UBA-CONICET), Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires (C1428EHA), Argentina
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Pablo Mammi;
Pablo Mammi
*Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE, UBA-CONICET), Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires (C1428EHA), Argentina
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Anabella Srebrow
Anabella Srebrow
2
*Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE, UBA-CONICET), Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellón 2, Buenos Aires (C1428EHA), Argentina
2To whom correspondence should be addressed (email asrebrow@fbmc.fcen.uba.ar).
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Publisher: Portland Press Ltd
Received:
January 08 2015
Revision Received:
March 13 2015
Accepted:
March 31 2015
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2015 Biochemical Society
2015
Biochem J (2015) 468 (2): 203–214.
Article history
Received:
January 08 2015
Revision Received:
March 13 2015
Accepted:
March 31 2015
Citation
Guillermo Risso, Matías Blaustein, Berta Pozzi, Pablo Mammi, Anabella Srebrow; Akt/PKB: one kinase, many modifications. Biochem J 1 June 2015; 468 (2): 203–214. doi: https://doi.org/10.1042/BJ20150041
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