Evidence map›Paper›PMID 18955495›Full record

ArticleThe Journal of biological chemistry2008

A chemical genomics study identifies Snf1 as a repressor of GCN4 translation.

Margaret K Shirra, Rhonda R McCartney, Chao Zhang, Kevan M Shokat, Martin C Schmidt, Karen M Arndt

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

29 citing papers in PubMed, 65 citations in OpenAlex.

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  19. Review
  20. SUMOylation regulates the SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013
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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

6 authors at 3 institutions in 1 country.

Margaret K ShirraDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Rhonda R McCartney
Chao Zhang
Kevan M Shokat
Martin C Schmidt
Karen M Arndt
University of Pittsburgh · USHoward Hughes Medical Institute · USUniversity of California, San Francisco · US

Funding

TRANSCRIPTION FACTOR MUTANTS OF YEASTR01GM052593 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARNDT, KAREN M · 1995 to 2020
$7.9M
MECHANISMS OF GLUCOSE SIGNAL TRANSDUCTION IN YEASTR01GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1995 to 2021
$7.1M
SPECIFIC INHIBITOR OF LCK TO PROBE T CELL SIGNALINGR01AI044009 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SHOKAT, KEVAN M. · 1998 to 2006
$2.1M
Role of the Snf1 protein kinase in regulating eukaryotic gene expressionR21DK074654 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARNDT, KAREN M · 2006 to 2007
$403k
DNA BINDING OF RECOMBINANT TFII D PROTEINSR29GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1991 to 1994
–
NIAID NIH HHS AI44009NIDDK NIH HHS DK74654NIDDK NIH HHS R21 DK074654NIGMS NIH HHS GM46443NIGMS NIH HHS GM52593
6 · The paper itself

Abstract

The Saccharomyces cerevisiae Snf1 kinase plays a critical role in recalibrating cellular metabolism in response to glucose depletion. Hundreds of genes show changes in expression levels when the SNF1 gene is deleted. However, cells can adapt to the absence of a specific gene when grown in long term culture. Here we apply a chemical genetic method to rapidly and selectively inactivate a modified Snf1 kinase using a pyrazolopyrimidine inhibitor. By allowing cells to adjust to a change in carbon source prior to inhibition of the Snf1 kinase activity, we identified a set of genes whose expression increased when Snf1 was inhibited. Prominent in this set are genes that are activated by Gcn4, a transcriptional activator of amino acid biosynthetic genes. Deletion of Snf1 increased Gcn4 protein levels without affecting its mRNA levels. The increased Gcn4 protein levels required the Gcn2 kinase and Gcn20, regulators of GCN4 translation. These data indicate that Snf1 functions upstream of Gcn20 to regulate control of GCN4 translation in S. cerevisiae.

Indexed as

Basic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsGene DeletionGene Expression Regulation, FungalProtein BiosynthesisProtein Kinase InhibitorsProtein Serine-Threonine KinasesPyrimidinesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsTriazolesBasic-Leucine Zipper Transcription FactorsDNA-Binding ProteinsGCN4 protein, S cerevisiaeProtein Kinase InhibitorsProtein Serine-Threonine KinasesPyrazolotriazolopyrimidinePyrimidinesSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesTranscription FactorsTriazoles

Identifiers

PMID18955495
PMCPMC2602918
OpenAlexW2087255503

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.