Ontology highlight
ABSTRACT:
SUBMITTER: Risso G
PROVIDER: S-EPMC3865012 | biostudies-literature | 2013 Oct
REPOSITORIES: biostudies-literature
Risso Guillermo G Pelisch Federico F Pozzi Berta B Mammi Pablo P Blaustein Matías M Colman-Lerner Alejandro A Srebrow Anabella A
Cell cycle (Georgetown, Tex.) 20130827 19
Akt/PKB is a key signaling molecule in higher eukaryotes and a crucial protein kinase in human health and disease. Phosphorylation, acetylation, and ubiquitylation have been reported as important regulatory post-translational modifications of this kinase. We describe here that Akt is modified by SUMO conjugation, and show that lysine residues 276 and 301 are the major SUMO attachment sites within this protein. We found that phosphorylation and SUMOylation of Akt appear as independent events. How ...[more]