Cited by 1,006Genomics and Chromatin DynamicsEpigenetics and DNA MethylationCancer-related gene regulation

Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications

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Yang, Xiang-Jiao, Seto, Edward·2008·Molecular Cell

Abstract

Lysine acetylation has emerged as a major posttranslational modification for histones. Crossregulation between this and other modifications is crucial in modulating chromatin-based transcriptional control and shaping inheritable epigenetic programs. In addition to histones, many other nuclear proteins and various cytoplasmic regulators are subject to lysine acetylation. This review focuses on recent findings pertinent to acetylation of nonhistone proteins and emphasizes how this modification might crosstalk with phosphorylation, methylation, ubiquitination, sumoylation, and others to form code-like multisite modification programs for dynamic control of cellular signaling under diverse conditions.

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Crossref · 10.1016/j.molcel.2008.07.002

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  • This enrichment possibly reflects the functional role of lysine acetylation in modulating protein degradation.

    “This possibly reflects the functional role of lysine acetylation in modulating protein degradation (23).”

    From Impact of regulatory variation from RNA to protein (2015) · cites this paper as [23]

  • Most human Tau acetylation sites identified were alternatively ubiquitinated.

    “Consistent with previous biochemical studies in mice (Morris et al., 2015; Yang and Seto, 2008), most of the human Tau acetylation sites identified were ubiquitinated alternatively (Figure 1E).”

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Authors
Yang, X.-J., & Seto, E.
Affiliations
  • McGill University Health Centre (CA)
  • Moffitt Cancer Center (US)
Corresponding author
  • Yang, Xiang-Jiao
  • Seto, Edward
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2008-08
Volume
31
Issue
4
Pages
449-461
ISSN
1097-2765 (ISSN-L)
OpenAlex
W2034614265
Cited by
1,006
References
110
Citations by year
2026: 25 · 2025: 35 · 2024: 32 · 2023: 34 · 2022: 50 · 2021: 45 · 2020: 47 · 2019: 39 · 2018: 53 · 2017: 56 · 2016: 55 · 2015: 69 · 2014: 84 · 2013: 80 · 2012: 92
FWCI
5.37
Type
journal article
Language
en
Open access
Locations
  • Molecular Cell (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Cancer Institute (R01CA109699)
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
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
Keywords
lysine acetylation, post-translational modification, histone modifications, non-histone proteins, chromatin, epigenetics, phosphorylation, methylation, ubiquitination, SUMOylation, signal transduction
MeSH terms
Acetylation, Acetyltransferases, Amidohydrolases, Amino Acid Sequence, Animals, Humans, Lysine, Molecular Sequence Data, Nuclear Proteins, Protein Processing, Post-Translational

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