Evidence map›Paper›PMID 22589305›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases.

Amparo Ruiz, Yang Liu, Xinjing Xu, Marian Carlson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020
    Article
  5. Article
  6. Review
  7. AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. SUMOylation regulates the SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
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

4 authors.

Amparo RuizDepartment of Genetics and Development, Columbia University, New York, NY 10032, USA.
Yang Liu
Xinjing Xu
Marian Carlson

Funding

REGULATION OF YEAST INVERTASE GENE EXPRESSIONR37GM034095 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI CARLSON, MARIAN B · 1996 to 2005
$3.1M
REGULATION OF YEAST INVERTASE GENE EXPRESSIONR01GM034095 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI CARLSON, MARIAN B · 1985 to 2014
$2.9M
NIGMS NIH HHS GM34095NIGMS NIH HHS R01 GM034095NIGMS NIH HHS R37 GM034095
6 · The paper itself

Abstract

The SNF1/AMP-activated protein kinases are αβγ-heterotrimers that sense and regulate energy status in eukaryotes. They are activated by phosphorylation of the catalytic Snf1/α subunit, and the Snf4/γ regulatory subunit regulates phosphorylation through adenine nucleotide binding. In Saccharomyces cerevisiae, the Snf1 subunit is phosphorylated on the activation-loop Thr-210 in response to glucose limitation. To assess the requirement of the heterotrimer for regulated Thr-210 phosphorylation, we examined Snf1 and a truncated Snf1 kinase domain (residues 1-309) that has partial Snf1 function. Snf1(1-309) does not interact with the β and Snf4/γ regulatory subunits, and its activity was independent of them in vivo. Phosphorylation of both Snf1 and Snf1(1-309) increased in response to glucose limitation in wild-type cells and in cells lacking β- and Snf4/γ-subunits. These results indicate that glucose regulation of activation-loop phosphorylation can occur by mechanism(s) that function independently of the regulatory subunits. We further show that the Reg1-Glc7 protein phosphatase 1 and Sit4 type 2A-like phosphatase are largely responsible for dephosphorylation of Thr-210 of Snf1(1-309). Together, these findings suggest that these two phosphatases mediate heterotrimer-independent regulation of Thr-210 phosphorylation.

Indexed as

AMP-Activated Protein KinasesEnzyme ActivationGlucoseImmunoblottingModels, BiologicalMutationPhosphorylationProtein MultimerizationProtein Phosphatase 1Protein Phosphatase 2Protein Serine-Threonine KinasesProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThreonineTranscription FactorsAMP-Activated Protein KinasesGLC7 protein, S cerevisiaeGlucoseProtein Phosphatase 1Protein Phosphatase 2Protein Serine-Threonine KinasesProtein SubunitsREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIT4 protein, S cerevisiaeSNF1-related protein kinasesSNF4 protein, S cerevisiaeThreonineTranscription Factors

Identifiers

PMID22589305
PMCPMC3365208

What OpenQuestion holds

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Registered trials

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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.