Cited by 341Ubiquitin and proteasome pathwaysHistone Deacetylase Inhibitors ResearchGenomics and Chromatin Dynamics

Identification of components of the murine histone deacetylase 6 complex: link between acetylation and ubiquitination signaling pathways

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Seigneurin-Berny, Daphné, Verdel, André, Curtet, Sandrine, Lemercier, Claudie, Garin, Jérôme, Rousseaux, Sophie, Khochbin, Saadi·2001·Molecular and Cellular Biology

Abstract

The immunopurification of the endogenous cytoplasmic murine histone deacetylase 6 (mHDAC6), a member of the class II HDACs, from mouse testis cytosolic extracts allowed the identification of two associated proteins. Both were mammalian homologues of yeast proteins known to interact with each other and involved in the ubiquitin signaling pathway: p97/VCP/Cdc48p, a homologue of yeast Cdc48p, and phospholipase A2-activating protein, a homologue of yeast UFD3 (ubiquitin fusion degradation protein 3). Moreover, in the C-terminal region of mHDAC6, a conserved zinc finger-containing domain named ZnF-UBP, also present in several ubiquitin-specific proteases, was discovered and was shown to mediate the specific binding of ubiquitin by mHDAC6. By using a ubiquitin pull-down approach, nine major ubiquitin-binding proteins were identified in mouse testis cytosolic extracts, and mHDAC6 was found to be one of them. All of these findings strongly suggest that mHDAC6 could be involved in the control of protein ubiquitination. The investigation of biochemical properties of the mHDAC6 complex in vitro further supported this hypothesis and clearly established a link between protein acetylation and protein ubiquitination.

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Crossref · 10.1128/mcb.21.23.8035-8044.2001

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  • HDAC6 also regulates the autophagy-dependent clearance of defective mitochondria, likely compromising lipid metabolism in Abca4−/− mice.

    “HDAC6 also regulates the autophagy-dependent clearance of defective mitochondria (Seigneurin-Berny et al., 2001), likely compromising lipid metabolism in Abca4−/− mice (discussed in more detail section 6).”

    From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Seigneurin-Berny et al., 2001

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Authors
Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S., & Khochbin, S.
Affiliations
  • Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Equipe Chromatine et Expression des Gènes, Institut Albert Bonniot, Facultéde Médecine, Domaine de la Merci
  • Inserm (FR)
  • Laboratoire de Chimie des Protéines, CEA
Corresponding author
Khochbin, Saadi
Venue
Molecular and Cellular Biology
Published
2001-12
Volume
21
Issue
23
Pages
8035-8044
ISSN
  • 0270-7306 (ISSN-L)
  • 1098-5549
OpenAlex
W2125568224
Cited by
335
References
38
Citations by year
2026: 8 · 2025: 5 · 2024: 6 · 2023: 10 · 2022: 8 · 2021: 11 · 2020: 14 · 2019: 9 · 2018: 15 · 2017: 17 · 2016: 12 · 2015: 9 · 2014: 15 · 2013: 16 · 2012: 15
FWCI
5.36
Type
journal article
Language
en
Open access
Locations
  • Molecular and Cellular Biology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, other-oa)
  • HAL (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • 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
Keywords
HDAC6, class II HDACs, protein acetylation, ubiquitination, ubiquitin-binding protein, ubiquitin-specific protease, protein degradation
MeSH terms
Histone Deacetylase 6, Valosin Containing Protein, Acetylation, Adenosine Triphosphatases, Animals, Enzyme Activation, Histone Deacetylases, Male, Molecular Sequence Data, Endopeptidases, Protein Binding, Proteins, Spermatogenesis, Testis, Ubiquitins, Signal Transduction, Zinc Fingers, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Cell Cycle Proteins, Macromolecular Substances, Mice, Ubiquitin-Specific Proteases

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