The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structural Basis for Assembly and Activation of the Heterotetrameric SAGA Histone H2B Deubiquitinase Module
Open accessAbstract
Summary Deubiquitinating enzymes (DUBs) regulate diverse cellular functions by cleaving ubiquitin from specific protein substrates. How their activities are modulated in various cellular contexts remains poorly understood. The yeast deubiquitinase Ubp8 protein is recruited and activated by the SAGA complex and, together with Sgf11, Sus1, and Sgf73, forms a DUB module responsible for deubiquitinating histone H2B during gene expression. Here we report the crystal structure of the complete SAGA DUB module, which features two functional lobes structurally coupled by Sgf73. In the “assembly lobe”, a long Sgf11 N-terminal helix is clamped onto the Ubp8 ZnF-UBP domain by Sus1. In the “catalytic lobe”, an Sgf11 C-terminal zinc finger domain binds to the Ubp8 catalytic domain next to its active site. Our structural and functional analyses reveal a central role of Sgf11 and Sgf73 in activating Ubp8 for deubiquitinating histone H2B and demonstrate how a DUB can be allosterically regulated by its non-substrate partners.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Henry, K. W., Wyce, A., Lo, W.-S., Duggan, L. J., Emre, N. C. T., Kao, C.-F., Pillus, L., Shilatifard, A., Osley, M. A., & Berger, S. L. (2003) · Genes & Development · doi:10.1101/gad.1144003 · Cited by 714
Zhang, X.-Y., Varthi, M., Sykes, S. M., Phillips, C., Warzecha, C., Zhu, W., Wyce, A., Thorne, A. W., Berger, S. L., & McMahon, S. B. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.015 · Cited by 427 · cited 2×
“Remarkably, USP22, the human ortholog of Ubp8, forms a similar SAGA DUB module and deubiquitinates both H2A and H2B (Zhang et al., 2008; Zhao et al., 2008).”
Hu, M., Gu, L., Li, M., Jeffrey, P. D., Gu, W., & Shi, Y. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040027 · Cited by 251
Cited by
Deubiquitylases From Genes to Organism
Clague, M. J., Barsukov, I., Coulson, J. M., Liu, H., Rigden, D. J., & Urbé, S. (2013) · Physiological Reviews · doi:10.1152/physrev.00002.2013 · Cited by 425
Lin, Z., Yang, H., Kong, Q., Li, J., Lee, S.-M., Gao, B., Dong, H., Wei, J., Song, J., Zhang, D. D., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.024 · Cited by 315
Henriksen, P., Wagner, S. A., Weinert, B. T., Sharma, S., Bačinskaja, G., Rehman, M., Juffer, A. H., Walther, T. C., Lisby, M., & Choudhary, C. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.017251 · Cited by 246
Sussman, R. T., Stanek, T. J., Esteso, P., Gearhart, J. D., Knudsen, K. E., & McMahon, S. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.469783 · Cited by 91
Ubiquitin-specific protease 22 is a deubiquitinase of CCNB1
Lin, Z., Tan, C., Qiu, Q., Kong, S., Yang, H., Zhao, F., Liu, Z., Li, J., Kong, Q., Gao, B., et al. (2015) · Cell Discovery · doi:10.1038/celldisc.2015.28 · Cited by 90
Metadata
- Authors
- Köhler, A., Zimmerman, E., Schneider, M., Hurt, E., & Zheng, N.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-05
- Volume
- 141
- Issue
- 4
- Pages
- 606-617
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2120619403
- Cited by
- 186
- References
- 4
- FWCI
- 5.67
- Type
- journal article
- Language
- en
- Open access
- bronze
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Structural Basis for Assembly and Activation of the Heterotetrameric SAGA Histone H2B Deubiquitinase Module. https://app.cochat.ai/papers/10.1016/j.cell.2010.04.026
- The paper
- Köhler, A., Zimmerman, E., Schneider, M., Hurt, E., & Zheng, N. (2010). Structural Basis for Assembly and Activation of the Heterotetrameric SAGA Histone H2B Deubiquitinase Module. Cell. https://doi.org/10.1016/j.cell.2010.04.026
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
