Akt Is S-Palmitoylated: A New Layer of Regulation for Akt

• DOI: 10.3389/fcell.2021.626404
• Publication Date: 2021-02-15T09:27:44Z
• Authors: Matías Blaustein; Estefanía Piegari; Camila Martínez C...; Antonella Vila; Analía Amante; María Victoria Ma...; Ari Zeida; Laurence Abrami; Mariela Veggetti; David A. Guertin; F. Gisou van der ...; María Martha Corvi; Alejandro Colman-...
• Keywords: Palmitoylation

The protein kinase Akt/PKB participates in a great variety of processes, including translation, cell proliferation and survival, as well malignant transformation viral infection. In the last few years, novel Akt posttranslational modifications have been found. However, how these modification patterns affect subcellular localization, target specificity and, general, function is not thoroughly understood. Here, we postulate experimentally demonstrate by acyl-biotin exchange (ABE) assay 3 H-palmitate metabolic labeling that S-palmitoylated, related to sorting throughout membranes. Mutating cysteine 344 into serine blocked S-palmitoylation diminished its phosphorylation at two key sites, T308 T450. Particularly, show palmitoylation-deficient increases recruitment cytoplasmic structures colocalize with lysosomes, process stimulated during autophagy. Finally, found Akt1 important for proper function, since Akt1-C344S was unable support adipocyte differentiation vitro. These results add an unexpected new layer already complex molecular code, improving our understanding decision-making mechanisms such death.