ArticleStructure (London, England : 1993)2012
A role for intersubunit interactions in maintaining SAGA deubiquitinating module structure and activity.
Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- UPS writes a new saga of SAGA.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Review
- Article
- Potent macrocycle inhibitors of the human SAGA deubiquitinating module.Cell chemical biology · 2022Article
- Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021Review
- The histone H4 basic patch regulates SAGA-mediated H2B deubiquitination and histone acetylation.The Journal of biological chemistry · 2020Article
- Active site alanine mutations convert deubiquitinases into high-affinity ubiquitin-binding proteins.EMBO reports · 2018Article
- DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis.eLife · 2018Article
- Whole-Genome Sequencing of Suppressor DNA Mixtures Identifies Pathways That Compensate for Chromosome Segregation Defects inG3 (Bethesda, Md.) · 2018Article
- Sharing the SAGA.Trends in biochemical sciences · 2017Review
- Dub3 inhibition suppresses breast cancer invasion and metastasis by promoting Snail1 degradation.Nature communications · 2017Article
- Recognition of ubiquitinated nucleosomes.Current opinion in structural biology · 2017Review
- Validation and correction of Zn-CysActa crystallographica. Section D, Structural biology · 2016Article
- Structural basis for histone H2B deubiquitination by the SAGA DUB module.Science (New York, N.Y.) · 2016Article
- Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity.Journal of molecular biology · 2015Article
- Deubiquitinases and the new therapeutic opportunities offered to cancer.Endocrine-related cancer · 2015Review
- Sus1p facilitates pre-initiation complex formation at the SAGA-regulated genes independently of histone H2B de-ubiquitylation.Journal of molecular biology · 2014Article
- The crystal structure of S. cerevisiae Sad1, a catalytically inactive deubiquitinase that is broadly required for pre-mRNA splicing.RNA (New York, N.Y.) · 2014Article
- Mechanisms for regulating deubiquitinating enzymes.Protein science : a publication of the Protein Society · 2014Review
- DNA binding by Sgf11 protein affects histone H2B deubiquitination by Spt-Ada-Gcn5-acetyltransferase (SAGA).The Journal of biological chemistry · 2014Article
- SAGA and SAGA-like SLIK transcriptional coactivators are structurally and biochemically equivalent.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The deubiquitinating module (DUBm) of the SAGA coactivator contains the Ubp8 isopeptidase, Sgf11, Sus1, and Sgf73, which form a highly interconnected complex. Although Ubp8 contains a canonical USP catalytic domain, it is only active when in complex with the other DUBm subunits. The Sgf11 zinc finger (Sgf11-ZnF) binds near the Ubp8 active site and is essential for full activity, suggesting that the Sgf11-ZnF helps maintain the active conformation of Ubp8. We report structural and solution studies showing that deletion of the Sgf11-ZnF destabilizes incorporation of Ubp8 within the DUBm, giving rise to domain swapping with a second complex and misaligning active site residues. Activating mutations in Ubp8 that partially restore activity in the absence of the Sgf11-ZnF promote the monomeric form of the DUBm. Our data suggest an unexpected role for Sgf11 in compensating for the absence of structural features that maintain the active conformation of Ubp8.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.