Lysine Acetylation: Codified Crosstalk with Other Posttranslational Modifications
Open accessAbstract
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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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).”
From Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease (2020) · cites this paper as Yang and Seto, 2008
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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)
- PMC
- PMC2551738
- 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
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1847 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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