Cited by 414Histone Deacetylase Inhibitors ResearchUbiquitin and proteasome pathwaysMicrotubule and mitosis dynamics

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HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination

Boyault, C, Sadoul, K, Pabion, M, Khochbin, S·2007·Oncogene

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Abstract

Histone deacetylase 6 (HDAC6) is a unique enzyme with specific structural and functional features. It is actively or stably maintained in the cytoplasm and is the only member, within the histone deacetylase family, that harbors a full duplication of its deacetylase homology region followed by a specific ubiquitin-binding domain at the C-terminus end. Accordingly, this deacetylase functions at the heart of a cellular regulatory mechanism capable of coordinating various cellular functions largely relying on the microtubule network. Moreover, HDAC6 action as a regulator of the HSP90 chaperone activity adds to the multifunctionality of the protein, and allows us to propose a critical role for HDAC6 in mediating and coordinating various cellular events in response to different stressful stimuli.

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Background
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Background
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Background
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Background
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“As a number of studies have demonstrated the regulatory role of HDAC6 in microtubule dynamics by tuning the tubulin acetylation/deacetylation (Boyault et al. , 2007; Liu et al. , 2015), we infer that an HPIP-HDAC6-tubulin axis may exist in breast cancer, although there is a gap between HPIP and…”
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Authors: Boyault, C., Sadoul, K., Pabion, M., & Khochbin, S.
Affiliations: Inserm (FR)
Corresponding author: Khochbin, S
ORCID: Boyault, C
Sadoul, K
Khochbin, S
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2007-08-13
Volume: 26
Issue: 37
Pages: 5468-5476
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1210614
OpenAlex: W2030185116
Cited by: 397
References: 85
Citations by year: 2026: 12 · 2025: 17 · 2024: 19 · 2023: 15 · 2022: 24 · 2021: 26 · 2020: 32 · 2019: 18 · 2018: 31 · 2017: 16 · 2016: 9 · 2015: 23 · 2014: 21 · 2013: 24 · 2012: 26
FWCI: 1.72
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Funders: Institut National Du Cancer
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: HDAC6, histone deacetylase, microtubule cytoskeleton, cytoskeleton, protein acetylation, ubiquitination, ubiquitin-binding domain, Hsp90 chaperone, signal transduction, stress response
MeSH terms: Acetylation, Animals, Cell Nucleus, Cytoskeleton, Enzyme Inhibitors, Histone Deacetylases, Humans, Protein Processing, Post-Translational, Signal Transduction, Protein Structure, Tertiary, Ubiquitin, Histone Deacetylase Inhibitors

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HDAC6, at the crossroads between cytoskeleton and cell signaling by acetylation and ubiquitination

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