Evidence map›Paper›PMID 17991748›Full record

ArticleThe Journal of biological chemistry2008

Access denied: Snf1 activation loop phosphorylation is controlled by availability of the phosphorylated threonine 210 to the PP1 phosphatase.

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

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 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

68 citing papers in PubMed, 136 citations in OpenAlex.

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  16. Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020
    Article
  17. Review
  18. Review
  19. Article
  20. Spontaneous mutations inMicrobial cell (Graz, Austria) · 2018
    Article

8 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

7 authors at 3 institutions in 1 country.

Eric M RubensteinDepartment of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Rhonda R McCartneyDepartment of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261.
Chao ZhangHoward Hughes Medical Institute and Department of Molecular and Cellular Pharmacology, University of California, San Francisco, San Francisco, California 94143.
Kevan M ShokatHoward Hughes Medical Institute and Department of Molecular and Cellular Pharmacology, University of California, San Francisco, San Francisco, California 94143.
Margaret K ShirraDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
Karen M ArndtDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260.
Martin C SchmidtDepartment of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261. Electronic address: mcs2@pitt.edu.
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 AI 44009NIAID NIH HHS R01 AI044009NIDDK NIH HHS DK 74654NIDDK NIH HHS R21 DK074654NIGMS NIH HHS GM 46443NIGMS NIH HHS GM 52593NIGMS NIH HHS R01 GM046443NIGMS NIH HHS R01 GM052593
6 · The paper itself

Abstract

Phosphorylation of the Saccharomyces cerevisiae Snf1 kinase activation loop is determined by the integration of two reaction rates: the rate of phosphorylation by upstream kinases and the rate of dephosphorylation by Glc7. The activities of the Snf1-activating kinases do not appear to be glucose-regulated, since immune complex kinase assays with each of the three Snf1-activating kinases show similar levels of activity when prepared from cells grown in either high or low glucose. In contrast, the dephosphorylation of the Snf1 activation loop was strongly regulated by glucose. When de novo phosphorylation of Snf1 was inhibited, phosphorylation of the Snf1 activation loop was found to be stable in low glucose but rapidly lost upon the addition of glucose. A greater than 10-fold difference in the rates of Snf1 activation loop dephosphorylation was detected. However, the activity of the Glc7-Reg1 phosphatase may not itself be directly regulated by glucose, since the Glc7-Reg1 enzyme was active in low glucose toward another substrate, the transcription factor Mig1. Glucose-mediated regulation of Snf1 activation loop dephosphorylation is controlled by changes in the ability of the Snf1 activation loop to act as a substrate for Glc7.

Indexed as

AMP-Activated Protein KinasesBlotting, WesternDNA-Binding ProteinsEnzyme ActivationGlucoseModels, BiologicalMultienzyme ComplexesPhosphoprotein PhosphatasesPhosphorylationProtein BindingProtein Phosphatase 1Protein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionAMP-Activated Protein KinasesDNA-Binding ProteinsGLC7 protein, S cerevisiaeGlucoseMIG1 protein, S cerevisiaeMultienzyme ComplexesPhosphoprotein PhosphatasesProtein Phosphatase 1Protein Serine-Threonine KinasesREG1 protein, S cerevisiaeRepressor ProteinsSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesThreonine

Identifiers

PMID17991748
PMCPMC3244878
OpenAlexW2067346106

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.