Acetylation and deacetylation of non-histone proteins

Glozak, Michele A.; Sengupta, Nilanjan; Zhang, Xiaohong; Seto, Edward

doi:10.1016/j.gene.2005.09.010

Cited by 1,584Histone Deacetylase Inhibitors ResearchGenomics and Chromatin DynamicsEpigenetics and DNA Methylation

Acetylation and deacetylation of non-histone proteins

Glozak, Michele A., Sengupta, Nilanjan, Zhang, Xiaohong, Seto, Edward·2005·Gene

DOI 10.1016/j.gene.2005.09.010

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Abstract

Since the first report of p53 as a non-histone target of a histone acetyltransferase (HAT), there has been a rapid proliferation in the description of new non-histone targets of HATs. Of these, transcription factors comprise the largest class of new targets. The substrates for HATs extend to cytoskeletal proteins, molecular chaperones and nuclear import factors. Deacetylation of these non-histone proteins by histone deacetylases (HDACs) opens yet another exciting new field of discovery in the role of the dynamic acetylation and deacetylation on cellular function. This review will focus on these non-histone targets of HATs and HDACs and the consequences of their modification.

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The mammalian HDAC family consists of 18 isoforms categorized into four major classes (Classes I-IV).
“The mammalian HDAC family consists of 18 isoforms categorized into four major classes (Classes I–IV) (Zhang et al., 2024; Glozak et al., 2005; Gallinari et al., 2007; Yang and Grégoire, 2005), as summarized in Table 1 (Vanaja et al., 2018; Johnstone, 2002; Gao et al., 2002; Tong et al., 2002; Hubbert et al., 2002).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Glozak et al., 2005
HDAC inhibitors exert neuroprotective effects through anti-inflammatory mechanisms such as reduced microglial activation and through non-transcriptional actions including microtubule acetylation-mediated support of axonal transport and plasticity.
“HDAC inhibitors exert neuroprotective effects through both anti-inflammatory mechanisms, such as reduced microglial activation, and non-transcriptional actions, including microtubule acetylation–mediated support of axonal transport and plasticity (Glozak et al., 2005; Chuang et al., 2009; Suh et al., 2010).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Glozak et al., 2005

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Authors: Glozak, M. A., Sengupta, N., Zhang, X., & Seto, E.
Affiliations: Moffitt Cancer Center (US)
Corresponding author: Seto, Edward
ORCID: Zhang, Xiaohong
Seto, Edward
Venue: Gene
Publisher: Elsevier BV
Published: 2005-12
Volume: 363
Pages: 15-23
ISSN: 0378-1119 (ISSN-L)
DOI: 10.1016/j.gene.2005.09.010
OpenAlex: W1975692560
Cited by: 1,584
References: 93
Citations by year: 2026: 28 · 2025: 44 · 2024: 57 · 2023: 51 · 2022: 67 · 2021: 68 · 2020: 76 · 2019: 89 · 2018: 68 · 2017: 86 · 2016: 99 · 2015: 97 · 2014: 101 · 2013: 99 · 2012: 110
FWCI: 4.71
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Gene (publishedVersion)
PubMed (publishedVersion)
Funders: Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
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
Keywords: protein acetylation, protein deacetylation, non-histone proteins, histone acetyltransferase, histone deacetylase, p53, transcription factors, cytoskeletal proteins, molecular chaperones
MeSH terms: Acetylation, Chromosomal Proteins, Non-Histone, Histone Deacetylases, Transcription Factors, Viral Proteins

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Acetylation and deacetylation of non-histone proteins

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