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Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?

Skeletal muscle insulin resistance, which increases the risk for developing various metabolic diseases, including type 2 diabetes, is a common metabolic disorder in obesity and aging. If potential treatments are to be developed to treat insulin resistance, then it is important to fully understand in...

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Detalles Bibliográficos
Autores principales: LaBarge, Samuel, Migdal, Christopher, Schenk, Simon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Korean Society for Molecular and Cellular Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4400303/
https://www.ncbi.nlm.nih.gov/pubmed/25824547
http://dx.doi.org/10.14348/molcells.2015.0020
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author LaBarge, Samuel
Migdal, Christopher
Schenk, Simon
author_facet LaBarge, Samuel
Migdal, Christopher
Schenk, Simon
author_sort LaBarge, Samuel
collection PubMed
description Skeletal muscle insulin resistance, which increases the risk for developing various metabolic diseases, including type 2 diabetes, is a common metabolic disorder in obesity and aging. If potential treatments are to be developed to treat insulin resistance, then it is important to fully understand insulin signaling and glucose metabolism. While recent large-scale “omics” studies have revealed the acetylome to be comparable in size to the phosphorylome, the acetylation of insulin signaling proteins and its functional relevance to insulin-stimulated glucose transport and glucose metabolism is not fully understood. In this Mini Review we discuss the acetylation status of proteins involved in the insulin signaling pathway and review their potential effect on, and relevance to, insulin action in skeletal muscle.
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spelling pubmed-44003032015-04-24 Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action? LaBarge, Samuel Migdal, Christopher Schenk, Simon Mol Cells Minireview Skeletal muscle insulin resistance, which increases the risk for developing various metabolic diseases, including type 2 diabetes, is a common metabolic disorder in obesity and aging. If potential treatments are to be developed to treat insulin resistance, then it is important to fully understand insulin signaling and glucose metabolism. While recent large-scale “omics” studies have revealed the acetylome to be comparable in size to the phosphorylome, the acetylation of insulin signaling proteins and its functional relevance to insulin-stimulated glucose transport and glucose metabolism is not fully understood. In this Mini Review we discuss the acetylation status of proteins involved in the insulin signaling pathway and review their potential effect on, and relevance to, insulin action in skeletal muscle. Korean Society for Molecular and Cellular Biology 2015-04 2015-03-31 /pmc/articles/PMC4400303/ /pubmed/25824547 http://dx.doi.org/10.14348/molcells.2015.0020 Text en © The Korean Society for Molecular and Cellular Biology. All rights reserved. This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-ShareAlike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/.
spellingShingle Minireview
LaBarge, Samuel
Migdal, Christopher
Schenk, Simon
Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?
title Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?
title_full Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?
title_fullStr Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?
title_full_unstemmed Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?
title_short Is Acetylation a Metabolic Rheostat that Regulates Skeletal Muscle Insulin Action?
title_sort is acetylation a metabolic rheostat that regulates skeletal muscle insulin action?
topic Minireview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4400303/
https://www.ncbi.nlm.nih.gov/pubmed/25824547
http://dx.doi.org/10.14348/molcells.2015.0020
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