Akt/PKB: One kinase, many modifications

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 a...

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Autores principales:	Risso, G., Blaustein, M., Pozzi, B., Mammi, P., Srebrow, A.
Formato:	JOUR
Materias:	Akt Post-translational modification Protein function Protein kinase B Signal transduction cysteine deubiquitinase lysine protein kinase B serine threonine tyrosine 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 Eukaryota Animals Humans Protein Processing, Post-Translational Proto-Oncogene Proteins c-akt
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_02646021_v468_n2_p203_Risso
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_02646021_v468_n2_p203_Risso
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spelling	todo:paper_02646021_v468_n2_p203_Risso2023-10-03T15:13:04Z Akt/PKB: One kinase, many modifications Risso, G. Blaustein, M. Pozzi, B. Mammi, P. Srebrow, A. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Risso, G. Blaustein, M. Pozzi, B. Mammi, P. Srebrow, A. 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.
format	JOUR
author	Risso, G. Blaustein, M. Pozzi, B. Mammi, P. Srebrow, A.
author_facet	Risso, G. Blaustein, M. Pozzi, B. Mammi, P. Srebrow, A.
author_sort	Risso, G.
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
url	http://hdl.handle.net/20.500.12110/paper_02646021_v468_n2_p203_Risso
work_keys_str_mv	AT rissog aktpkbonekinasemanymodifications AT blausteinm aktpkbonekinasemanymodifications AT pozzib aktpkbonekinasemanymodifications AT mammip aktpkbonekinasemanymodifications AT srebrowa aktpkbonekinasemanymodifications
_version_	1807317562379206656

Akt/PKB: One kinase, many modifications

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