The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
Identification of Components of the Murine Histone Deacetylase 6 Complex: Link between Acetylation and Ubiquitination Signaling Pathways
Open accessAbstract
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“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
Citations
Cites
SMART, a simple modular architecture research tool: Identification of signaling domains
Schultz, J., Milpetz, F., Peer Bork, B., & Ponting, C. P. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.5857 · Cited by 3,577
UBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,706
Spermatogenic cells of the prepuberal mouse: isolation and morphological characterization
Bellve, A., Cavicchia, J. C., Millette, C. F., O'Brien, D. A., Bhatnagar, Y. M., & Dym, M. (1977) · The Journal of Cell Biology · doi:10.1083/jcb.74.1.68 · Cited by 1,386
A Novel Ubiquitination Factor, E4, Is Involved in Multiubiquitin Chain Assembly
Koegl, M., Hoppe, T., Schlenker, S., Ulrich, H. D., Mayer, T. U., & Jentsch, S. (1999) · Cell · doi:10.1016/s0092-8674(00)80574-7 · Cited by 1,074
A Proteolytic Pathway That Recognizes Ubiquitin as a Degradation Signal
Johnson, E. S., Philip, C. M., Ota, I. M., & Varshavsky, A. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17442 · Cited by 830
Regulation of E2F1 activity by acetylation
Martínez‐Balbás, M. A., Bauer, U., Nielsen, S. J., Brehm, A., & Kouzarides, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.662 · Cited by 670
Huibregtse, J. M., Scheffner, M., & Howley, P. M. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.2.775 · Cited by 553
The Human Histone Deacetylase Family
Gray, S. G., & Ekström, T. J. (2001) · Experimental Cell Research · doi:10.1006/excr.2000.5080 · Cited by 544
The AAA team: related ATPases with diverse functions
Patel, S. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(97)01212-9 · Cited by 519
Separation of mouse spermatogenic cells by sedimentation velocity
Romrell, L. J., Bellvé, A. R., & Fawcett, D. W. (1976) · Developmental Biology · doi:10.1016/0012-1606(76)90262-1 · Cited by 502
Cited by
Sorted by citations
Items 301–341 of 341
An Overview of Epigenetic Mechanisms in Health and Disease
Westerland, C., & Karagiannis, T. C. (2014) · Springer eBooks · doi:10.1007/978-1-4939-0706-9_3
Histone deacetylases and their co-regulators in Schizosaccharomyces pombe
Silverstein, R. A. (2007) · Figshare
Einfluss der Histon Deacetylase 6 auf den Glucocorticoid Rezeptor-vermittelten Glucosestoffwechsel
Winkler, R. (2012) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-4337
Can changes in SR protein acetylation affect alternative splicing?
Knupp, H. E. (2011) · doi:10.33915/etd.525
The role of autophagy in clearance of protein aggregates
Isakson, P. (2011) · NORA - Norwegian Open Research Archives
Epigenetic repression of the NFATc1 transcription factor in human lymphomas
Akimzhanov, A. M. (2005) · Online Publication Service of Würzburg University (Würzburg University)
Folco, E. G., Brancaz, M.-V., Belly, A., & Nonchev, S. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/245423
The Role of Microtubule End Structure in Microtubule Acetylation and Dynamics
Coombes, C. E. (2016) · University of Minnesota Digital Conservancy (University of Minnesota)
Ito, A., & Yoshida, M. (2017) · Springer eBooks · doi:10.1007/978-4-431-56529-1_3
Epigenetics and Muscle Dysfunction in Chronic Obstructive Pulmonary Disease
Barreiro, E. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-800802-7.00004-6
Sun, Q. M. C., ZhaoGuangjie, C., & Cai, S. (2011)
Targeting (de)acetylation: A Diversity of Mechanism and Disease
Quaas, C. E., & Long, D. T. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00076-1
Histone Deacetylase Inhibitors
Sefhore, O., & Ling, S. (2021) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-030-73440-4_7
p97 and Ubiquitin: A Complex Story
Briggs, L. C., Dreveny, I., Pye, V. E., Beuron, F., McKeown, C. F., Zhang, X., & Freemont, P. S. (2007) · doi:10.1002/9783527619320.ch7b
Sen, R. (2003) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1015087.195800
Modulation of Histone Deacetylases Attenuates the Pathogenesis of Alzheimer's disease
Govindarajan, N. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-449
Histone Deacetylase 6 at Crossroads of Invection and Innate Immunity
Moreno-Gonzalo, O. (2018) · doi:10.4321/repisalud.7741
Dynamic profiling of the aggresome processing pathwayPreprint
Ghosh, S., Wang, L., Heß, D., Iešmantavičius, V., Englinger, J., Cao, C., Matthias, G., Seebacher, J., & Matthias, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.30.684516
ETUDE DE LA DEACETYLASE HDAC6 : UNE ENZYME MULTIFONCTIONNELLE
Gilquin, B. (2005) · OpenGrey (Institut de l'Information Scientifique et Technique)
Cabrera-Rodríguez, R., Pons-Grífols, A., Pernas, M., Casado, C., Trujillo‐González, R., Lorenzo-Sánchez, I., Reyes-Castañeda, I., Trinité, B., Blanco, J., & Valenzuela-Fernández, A. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02762-x
Rôle d'HDAC6 et de VCP dans la réponse au stress thermique. Implications dans l'IBMPFD
Pernet, L. (2014) · theses.fr (ABES) · doi:10.70675/47616bc9zd164z44b3z889cze4a70ebf46b9
Chatterjee, S. (2020) · theses.fr (ABES) · doi:10.70675/5d269afcz42aez4bd5zaf6cz373fc60b5595
Rôle de l'histone désacétylase HDAC6 au cours de l'érythropoïèse humaine
Vong, P. (2022) · theses.fr (ABES) · doi:10.70675/699e8d9bz5404z43f6zabe7zdd0f0b6c8c42
Yang, C., Xu, D., Zhu, Z., Kang, Z., Ren, K., Yang, Y., Huang, Y., Zhang, W. E., Che, J., Xu, X., et al. (2026) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2026084
Peng, J., Zhao, Q., Yu, C., Liu, W., Yu, X., Qin, P., Liu, Y., Niu, H., Sun, J., Xue, H., et al. (2026) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2026.110034
Zinc-finger ubiquitin-binding domain of histone deacetylase 6 modulates Tau structure and function
Balmik, A. A., & Chinnathambi, S. (2026) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2026.05.036
BindingDB (2024) · UC San Diego · doi:10.7270/q26t0rwh
BindingDB Entry 50001528: Discovery of a fluorescent probe with HDAC6 selective inhibition.
BindingDB (2020) · UC San Diego · doi:10.7270/q2028v2k
BindingDB (2026) · UC San Diego · doi:10.7270/q23n2879
Covalent Protein Modification as a Mechanism for Dynamic Recruitment of Specific Interactors
Bertos, N., Sangwan, V., Yang, X., & Park, M. (2010) · Springer eBooks · doi:10.1007/978-1-4419-6382-6_11
Metadata
- 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
- Publisher
- Informa UK Limited
- Published
- 2001-12
- Volume
- 21
- Issue
- 23
- Pages
- 8035-8044
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC99970
- 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
- green
- www.ncbi.nlm.nih.gov
- 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
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review