Evidence map›Paper›PMID 15657442›Full record

ArticleMolecular and cellular biology2005

The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex.

Kenneth K Lee, Laurence Florens, Selene K Swanson, Michael P Washburn, Jerry L Workman

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
5.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

93 citing papers in PubMed, 163 citations in OpenAlex.

  1. Sus1 Modulates Chromatin Remodeling and Gene Expression via the Cell Wall Integrity Pathway in Saccharomyces cerevisiae.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  2. Review
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  6. TheFrontiers in microbiology · 2022
    Article
  7. Review
  8. Role of UPP pathway in amelioration of diabetes-associated complications.Environmental science and pollution research international · 2021
    Review
  9. The biochemical and genetic discovery of the SAGA complex.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

33 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Kenneth K LeeStowers Institute for Medical Research, 1000 E. 50th Street, Kansas City, MO 64110, USA.
Laurence Florens
Selene K Swanson
Michael P Washburn
Jerry L Workman
Stowers Institute for Medical Research · US

Funding

COPPER METALLO-BIOCHEMISTRY IN SACCHAROMYCES CEREVISIAER01GM046787 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI KOSMAN, DANIEL J. · 1992 to 2002
$804k
NIGMS NIH HHS GM 46787
6 · The paper itself

Abstract

Covalent modifications of the histone tails and the cross talk between these modifications are hallmark features of gene regulation. The SAGA histone acetyltransferase complex is one of the most well-characterized complexes involved in these covalent modifications. The recent finding that the removal of the ubiquitin group from H2B is performed by a component of SAGA, Ubp8, is intriguing as it assigns two posttranslation modification processes to one complex. In this work, we characterize the association of Ubp8 with SAGA and the effect that acetylation and deubiquitylation have on one another in vitro and in vivo. We found not only that Ubp8 is a part of the SAGA complex, but also that its deubiquitylation activity requires Ubp8's association with SAGA. Furthermore, we found that the Ubp8 association with SAGA requires Sgf11 and that this requirement is reciprocal. We also found that the acetylation and deubiquitylation activities of SAGA are independent of one another. However, we found that preacetylating histone H2B inhibited subsequent deubiquitylation. Additionally, we found that increasing the ubiquitylation state of H2B inhibited the expression of the ARG1 gene, whose repression was previously shown to require the RAD6 ubiquitin ligase. Taken together, these data indicate that the expression of some genes, including ARG1, is regulated by a balance of histone H2B ubiquitylation in the cell.

Indexed as

AcetylationGene Expression Regulation, FungalHistonesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsTranscription, GeneticUbiquitinHistonesSaccharomyces cerevisiae ProteinsSGF11 protein, S cerevisiaeTranscription FactorsUbiquitin

Identifiers

PMID15657442
PMCPMC544014
OpenAlexW2107100789

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.