AMP-activated protein kinase regulates GLUT4 transcription by phosphorylating histone deacetylase 5
Open accessAbstract
OBJECTIVE: Insulin resistance associated with obesity and diabetes is ameliorated by specific overexpression of GLUT4 in skeletal muscle. The molecular mechanisms regulating skeletal muscle GLUT4 expression remain to be elucidated. The purpose of this study was to examine these mechanisms. RESEARCH DESIGN AND METHODS AND RESULTS: Here, we report that AMP-activated protein kinase (AMPK) regulates GLUT4 transcription through the histone deacetylase (HDAC)5 transcriptional repressor. Overexpression of HDAC5 represses GLUT4 reporter gene expression, and HDAC inhibition in human primary myotubes increases endogenous GLUT4 gene expression. In vitro kinase assays, site-directed mutagenesis, and site-specific phospho-antibodies establish AMPK as an HDAC5 kinase that targets S259 and S498. Constitutively active but not dominant-negative AMPK and 5-aminoimidazole-4-carboxamide-1-beta-D-ribonucleoside (AICAR) treatment in human primary myotubes results in HDAC5 phosphorylation at S259 and S498, association with 14-3-3 isoforms, and H3 acetylation. This reduces HDAC5 association with the GLUT4 promoter, as assessed through chromatin immunoprecipitation assays and HDAC5 nuclear export, concomitant with increases in GLUT4 gene expression. Gene reporter assays also confirm that the HDAC5 S259 and S498 sites are required for AICAR induction of GLUT4 transcription. CONCLUSIONS: These data reveal a signal transduction pathway linking cellular energy charge to gene transcription directed at restoring cellular and whole-body energy balance and provide new therapeutic targets for the treatment and management of insulin resistance and type 2 diabetes.
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Nuclear export of HDAC5 leads to a relaxation of the chromatin and, in an unknown manner, leads to increases in transcription of GLUT4.
“The nuclear export of HDAC5 therefore leads to a relaxation of the chromatin and in an unknown manner leads to increases in transcription of GLUT4 [30].”
From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [30]
AMPK can translocate to the nucleus where it regulates histone deacetylases, transcription factors and transcriptional co-activators such as HDAC5, MEF2 and PGC-1α.
“In a feed forward fashion AMPK can translocate to the nucleus [24,27] where it regulates Histone de-aceytlases, transcription factors and transcriptional co-activators such as histone deacetylase 5 (HDAC5), myocyte enhancing factor 2 (MEF2) and peroxisome proliferator activated receptor-γ co-activator-1α (PGC-1α) respectively (Figure 1) [28][29][30].”
From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [30]
AMPK-dependent regulation of HDAC5 leads to the nuclear export of this de-acetylase.
“The AMPK dependent regulation of HDAC5 leads to the nuclear export of this de-acetylase [30].”
From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [30]
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- Authors
- McGee, S. L., van Denderen, B. J. W., Howlett, K. F., Mollica, J., Schertzer, J. D., Kemp, B. E., & Hargreaves, M.
- Affiliations
- Deakin University (AU)
- St. Vincent’s Institute, Fitzroy, Australia
- The University of Melbourne (AU)
- Commonwealth Scientific and Industrial Research Organisation (AU)
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 2008-04-01
- Volume
- 57
- Issue
- 4
- Pages
- 860-867
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2170255149
- Cited by
- 455
- References
- 45
- Citations by year
- 2026: 13 · 2025: 21 · 2024: 16 · 2023: 23 · 2022: 14 · 2021: 26 · 2020: 35 · 2019: 24 · 2018: 28 · 2017: 31 · 2016: 29 · 2015: 31 · 2014: 32 · 2013: 26 · 2012: 22
- FWCI
- 11.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council
- National Health and Medical Research Council (400446)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- AMPK, GLUT4, HDAC5, skeletal muscle, insulin resistance, type 2 diabetes, transcriptional regulation, 14-3-3 proteins, histone H3 acetylation, AICAR, energy balance, myotubes
- MeSH terms
- Adult, Biopsy, Needle, Histone Deacetylases, Humans, Kinetics, Male, Multienzyme Complexes, Phosphorylation, Plasmids, RNA, Transcription, Genetic, Polymerase Chain Reaction, Protein Serine-Threonine Kinases, Muscle, Skeletal, Cell Culture Techniques, Glucose Transporter Type 4, AMP-Activated Protein Kinases
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