Cited by 178Genomics and Chromatin DynamicsEpigenetics and DNA MethylationSirtuins and Resveratrol in Medicine

The Metabolic Impact on Histone Acetylation and Transcription in Ageing

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Peleg, Shahaf, Feller, Christian, Ladurner, Andreas G., Imhof, Axel·2016·Trends in Biochemical Sciences

Abstract

Loss of cellular homeostasis during aging results in altered tissue functions and leads to a general decline in fitness and, ultimately, death. As animals age, the control of gene expression, which is orchestrated by multiple epigenetic factors, degenerates. In parallel, metabolic activity and mitochondrial protein acetylation levels also change. These two hallmarks of aging are effectively linked through the accumulating evidence that histone acetylation patterns are susceptible to alterations in key metabolites such as acetyl-CoA and NAD(+), allowing chromatin to function as a sensor of cellular metabolism. In this review we discuss experimental data supporting these connections and provide a context for the possible medical and physiological relevance.

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Crossref · 10.1016/j.tibs.2016.05.008

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  • Ubiquitination, sumoylation, O-GlcNAcylation, and ADP-ribosylation can have varying influences on transcriptional dysregulation.

    “while post-translational modifications like ubiquitination, sumoylation, O-GlcNAcylation, and ADP-ribosylation, can have varying influences on transcriptional dysregulation (Pal and Tyler 2016, Peleg et al. 2016).”

    From Benefits of Metformin in Attenuating the Hallmarks of Aging (2020) · cites this paper as Peleg et al. 2016

  • Histone acetylation and phosphorylation can lead to active transcription, loss of cellular homeostasis and age-associated metabolic decline.

    “Histone modifications such as acetylation and phosphorylation can lead to active transcription, loss of cellular homeostasis and age-associated metabolic decline”

    From Benefits of Metformin in Attenuating the Hallmarks of Aging (2020) · cites this paper as Peleg et al. 2016

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  1. [31]31. [Jacobson, R.H. et al. (2000) Structure and function of a human TAFII250 double bromodomain module. Science 288, 1422 -1425](http://refhub.elsevier.com/S0968-0004(16)30040-8/sbref0795)

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Authors
Peleg, S., Feller, C., Ladurner, A. G., & Imhof, A.
Affiliations
  • Ludwig-Maximilians-Universität München (DE)
  • ETH Zurich (CH)
  • Center for Integrated Protein Science Munich (DE)
Corresponding author
  • Peleg, Shahaf
  • Imhof, Axel
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2016-08
Volume
41
Issue
8
Pages
700-711
ISSN
0968-0004 (ISSN-L)
OpenAlex
W2418484636
Cited by
178
References
130
Citations by year
2026: 12 · 2025: 10 · 2024: 13 · 2023: 21 · 2022: 22 · 2021: 23 · 2020: 18 · 2019: 27 · 2018: 11 · 2017: 16 · 2016: 5
FWCI
1.78
Type
journal article
Language
en
Open access
Locations
  • Trends in Biochemical Sciences (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Repository for Publications and Research Data (ETH Zurich) (submittedVersion, cc-by)
  • ETH Zürich Research Collection
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
  • Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Keywords
histone acetylation, aging, cellular metabolism, acetyl-CoA, NAD+, mitochondrial protein acetylation, epigenetic regulation, chromatin, gene expression, metabolic homeostasis
MeSH terms
Acetylation, Aging, Animals, Histones, Humans, Transcription, Genetic

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