Evidence map›Paper›PMID 21628526›Full record

ArticleMolecular and cellular biology2011

Ubp8 and SAGA regulate Snf1 AMP kinase activity.

Marenda A Wilson, Evangelia Koutelou, Calley Hirsch, Kadir Akdemir, Andria Schibler, Michelle Craig Barton, Sharon Y R Dent

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  8. Deubiquitination in prostate cancer progression: role of USP22.Journal of cancer metastasis and treatment · 2020
    Article
  9. Review
  10. The Histone Acetyltransferase Gcn5 Positively Regulates T Cell Activation.Journal of immunology (Baltimore, Md. : 1950) · 2017
    Article
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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

7 authors at 1 institution in 1 country.

Marenda A WilsonDepartment of Biochemistry and Molecular Biology, Center forCancer Epigenetics, The University of Texas MD Anderson Cancer Center, 1515 Holcombe Blvd, Box 1000, Houston, Texas 77030, USA.
Evangelia Koutelou
Calley Hirsch
Kadir Akdemir
Andria Schibler
Michelle Craig Barton
Sharon Y R Dent
The University of Texas MD Anderson Cancer Center · US

Funding

ORGANIZATION OF CHROMATIN BY GLOBAL REGULATORS IN YEASTR01GM051189 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI DENT, SHARON Y. R. · 1994 to 2008
$2.1M
MOLECULAR BASIS OF DIFFERENTIATION AND DEVELOPMENTT32HD007325 · NICHD · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KLEIN, WILLIAM H. · 1986 to 2011
$2.1M
NICHD NIH HHS 2 T32 HD07325NICHD NIH HHS T32 HD007325NIGMS NIH HHS R01 GM051189NIGMS NIH HHS R01GM51189
6 · The paper itself

Abstract

Posttranslational modifications of histone proteins play important roles in the modulation of gene expression. The Saccharomyces cerevisiae (yeast) 2-MDa SAGA (Spt-Ada-Gcn5) complex, a well-studied multisubunit histone modifier, regulates gene expression through Gcn5-mediated histone acetylation and Ubp8-mediated histone deubiquitination. Using a proteomics approach, we determined that the SAGA complex also deubiquitinates nonhistone proteins, including Snf1, an AMP-activated kinase. Ubp8-mediated deubiquitination of Snf1 affects the stability and phosphorylation state of Snf1, thereby affecting Snf1 kinase activity. Others have reported that Gal83 is phosphorylated by Snf1, and we found that deletion of UBP8 causes decreased phosphorylation of Gal83, which is consistent with the effects of Ubp8 loss on Snf1 kinase functions. Overall, our data indicate that SAGA modulates the posttranslational modifications of Snf1 in order to fine-tune gene expression levels.

Indexed as

AcetylationAMP-Activated Protein KinasesEndopeptidasesGene Expression Regulation, FungalHistone AcetyltransferasesHistonesp300-CBP-Associated FactorPhosphorylationPlasmidsProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsUbiquitinationAMP-Activated Protein KinasesEndopeptidasesGCN5 protein, S cerevisiaeHistone AcetyltransferasesHistonesp300-CBP-Associated FactorProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeSNF1-related protein kinasesTrans-ActivatorsUBP8 protein, S cerevisiae

Identifiers

PMID21628526
PMCPMC3147604
OpenAlexW2128139629

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.