Evidence map›Paper›PMID 24019512›Full record

ArticleThe Journal of biological chemistry2013

Ptc1 protein phosphatase 2C contributes to glucose regulation of SNF1/AMP-activated protein kinase (AMPK) in Saccharomyces cerevisiae.

Amparo Ruiz, Xinjing Xu, Marian Carlson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
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  10. Review
  11. Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. SUMOylation represses SnRK1 signaling in Arabidopsis.The Plant journal : for cell and molecular biology · 2016
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

3 authors at 1 institution in 1 country.

Amparo RuizFrom the Department of Genetics and Development, Columbia University, New York, New York 10032.
Xinjing Xu
Marian Carlson
Columbia University · US

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 (AMPKs) function in energy regulation in eukaryotic cells. SNF1/AMPKs are αβγ heterotrimers that are activated by phosphorylation of the activation loop Thr on the catalytic subunit. Protein kinases that activate SNF1/AMPK have been identified, but the protein phosphatases responsible for dephosphorylation of the activation loop are less well defined. For Saccharomyces cerevisiae SNF1/AMPK, Reg1-Glc7 protein phosphatase 1 and Sit4 type 2A-related phosphatase function together to dephosphorylate Thr-210 on the Snf1 catalytic subunit during growth on high concentrations of glucose; reg1Δ and sit4Δ single mutations do not impair dephosphorylation when inappropriate glycogen synthesis, also caused by these mutations, is blocked. We here present evidence that Ptc1 protein phosphatase 2C also has a role in dephosphorylation of Snf1 Thr-210 in vivo. The sit4Δ ptc1Δ mutant exhibited partial defects in regulation of the phosphorylation state of Snf1. The reg1Δ ptc1Δ mutant was viable only when expressing mutant Snf1 proteins with reduced kinase activity, and Thr-210 phosphorylation of the mutant SNF1 heterotrimers was substantially elevated during growth on high glucose. This evidence, together with findings on the reg1Δ sit4Δ mutant, indicates that although Reg1-Glc7 plays the major role, all three phosphatases contribute to maintenance of the Snf1 activation loop in the dephosphorylated state during growth on high glucose. Ptc1 has overlapping functions with Reg1-Glc7 and Sit4 in glucose regulation of SNF1/AMPK and cell viability.

Indexed as

AMP-Activated Protein KinasesCatalytic DomainGene DeletionGlucosePhosphorylationProtein Phosphatase 1Protein Phosphatase 2Protein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAMP-Activated Protein KinasesGLC7 protein, S cerevisiaeGlucoseProtein Phosphatase 1Protein Phosphatase 2Protein Serine-Threonine KinasesPTC1 protein, S cerevisiaeREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIT4 protein, S cerevisiaeSNF1-related protein kinasesAMP-activated Kinase (AMPK)GlucosePhosphorylationProtein PhosphataseYeast Genetics

Identifiers

PMID24019512
PMCPMC3829418
OpenAlexW2022835332

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.