The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes
Open accessAbstract
Histone deacetylases (HDACs) are thought to function as critical mediators of transcriptional repression. However, the physiological targets and posttranslational modifications of the class II HDACs are largely unknown. Here we show that the C terminus of HDAC 6 is both necessary and sufficient for specific association with polyubiquitin. This region contains a putative zinc finger but lacks significant similarity to other known ubiquitin binding domains. Thus, we have designated this region as a PAZ domain, for P olyubiquitin A ssociated Z inc finger. Although the PAZ domain possesses homology with the zinc finger of deubiquitinating enzymes, it is dispensable for the deubiquitinating activity we find associated with HDAC6 following immunopurification. We also show that both HDAC 5 and HDAC 6 are ubiquitinated in vitro and in vivo . However, both of these proteins are stable in vivo and do not appear to be targeted for rapid degradation by the proteasome. Thus, HDAC6 is linked to the ubiquitin system via ubiquitin conjugation, polyubiquitin binding, and copurification with deubiquitinating enzymes.
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Cites
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403
Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., & Chen, Z. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00126-4 · Cited by 1,872
Signaling to Chromatin through Histone Modifications
Cheung, P., Allis, C. D., & Sassone-Corsi, P. (2000) · Cell · doi:10.1016/s0092-8674(00)00118-5 · Cited by 989
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770
Recruitment of a 19 S Proteasome Subcomplex to an Activated Promoter
Gonzalez, F., Delahodde, A., Kodadek, T., & Johnston, S. A. (2002) · Science · doi:10.1126/science.1069490 · Cited by 338
Seigneurin-Berny, D., Verdel, A., Curtet, S., Lemercier, C., Garin, J., Rousseaux, S., & Khochbin, S. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8035-8044.2001 · Cited by 335
Cited by
Kawaguchi, Y., Kovacs, J. J., McLaurin, A., Vance, J. M., Ito, A., & Yao, T.-P. (2003) · Cell · doi:10.1016/s0092-8674(03)00939-5 · Cited by 1,524
Gregoretti, I., Lee, Y.-M., & Goodson, H. V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.02.006 · Cited by 1,456
TAB2 and TAB3 Activate the NF-κB Pathway through Binding to Polyubiquitin Chains
Kanayama, A., Seth, R. B., Sun, L., Ea, C.-K., Hong, M., Shaito, A., Chiu, Y.-H., Deng, L., & Chen, Z. J. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.008 · Cited by 888
Bali, P., Pranpat, M., Bradner, J., Balasis, M., Fiskus, W., Guo, F., Rocha, K., Kumaraswamy, S., Boyapalle, S., Atadja, P., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500186200 · Cited by 755
How the ubiquitin–proteasome system controls transcription
Muratani, M., & Tansey, W. P. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1049 · Cited by 693
Metadata
- Authors
- Hook, S. S., Orian, A., Cowley, S. M., & Eisenman, R. N.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-09-27
- Volume
- 99
- Issue
- 21
- Pages
- 13425-13430
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2146620343
- Cited by
- 224
- References
- 7
- FWCI
- 3.35
- Type
- journal article
- Language
- en
- Open access
- green
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- Hook, S. S., Orian, A., Cowley, S. M., & Eisenman, R. N. (2002). Histone deacetylase 6 binds polyubiquitin through its zinc finger (PAZ domain) and copurifies with deubiquitinating enzymes. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.172511699
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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