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spelling paper:paper_02646021_v468_n2_p203_Risso2023-06-08T15:23:16Z Akt/PKB: One kinase, many modifications Akt Post-translational modification Protein function Protein kinase B Signal transduction cysteine deubiquitinase lysine protein kinase B serine threonine tyrosine protein kinase B amino acid sequence down regulation enzyme activity enzyme glycosylation enzyme metabolism enzyme phosphorylation enzyme regulation enzyme specificity human nonhuman priority journal protein acetylation protein degradation protein function protein processing proteomics Review signal transduction sumoylation ubiquitination animal metabolism protein processing Eukaryota Animals Humans Protein Processing, Post-Translational Proto-Oncogene Proteins c-akt 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 posttranslational 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. © The Authors Journal compilation © 2015 Biochemical Society. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v468_n2_p203_Risso http://hdl.handle.net/20.500.12110/paper_02646021_v468_n2_p203_Risso
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Akt
Post-translational modification
Protein function
Protein kinase B
Signal transduction
cysteine
deubiquitinase
lysine
protein kinase B
serine
threonine
tyrosine
protein kinase B
amino acid sequence
down regulation
enzyme activity
enzyme glycosylation
enzyme metabolism
enzyme phosphorylation
enzyme regulation
enzyme specificity
human
nonhuman
priority journal
protein acetylation
protein degradation
protein function
protein processing
proteomics
Review
signal transduction
sumoylation
ubiquitination
animal
metabolism
protein processing
Eukaryota
Animals
Humans
Protein Processing, Post-Translational
Proto-Oncogene Proteins c-akt
spellingShingle Akt
Post-translational modification
Protein function
Protein kinase B
Signal transduction
cysteine
deubiquitinase
lysine
protein kinase B
serine
threonine
tyrosine
protein kinase B
amino acid sequence
down regulation
enzyme activity
enzyme glycosylation
enzyme metabolism
enzyme phosphorylation
enzyme regulation
enzyme specificity
human
nonhuman
priority journal
protein acetylation
protein degradation
protein function
protein processing
proteomics
Review
signal transduction
sumoylation
ubiquitination
animal
metabolism
protein processing
Eukaryota
Animals
Humans
Protein Processing, Post-Translational
Proto-Oncogene Proteins c-akt
Akt/PKB: One kinase, many modifications
topic_facet Akt
Post-translational modification
Protein function
Protein kinase B
Signal transduction
cysteine
deubiquitinase
lysine
protein kinase B
serine
threonine
tyrosine
protein kinase B
amino acid sequence
down regulation
enzyme activity
enzyme glycosylation
enzyme metabolism
enzyme phosphorylation
enzyme regulation
enzyme specificity
human
nonhuman
priority journal
protein acetylation
protein degradation
protein function
protein processing
proteomics
Review
signal transduction
sumoylation
ubiquitination
animal
metabolism
protein processing
Eukaryota
Animals
Humans
Protein Processing, Post-Translational
Proto-Oncogene Proteins c-akt
description 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 posttranslational 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. © The Authors Journal compilation © 2015 Biochemical Society.
title Akt/PKB: One kinase, many modifications
title_short Akt/PKB: One kinase, many modifications
title_full Akt/PKB: One kinase, many modifications
title_fullStr Akt/PKB: One kinase, many modifications
title_full_unstemmed Akt/PKB: One kinase, many modifications
title_sort akt/pkb: one kinase, many modifications
publishDate 2015
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v468_n2_p203_Risso
http://hdl.handle.net/20.500.12110/paper_02646021_v468_n2_p203_Risso
_version_ 1768545140087980032