Evidence map›Paper›PMID 21464305›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase.

Amparo Ruiz, Xinjing Xu, Marian Carlson

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 85 citations in OpenAlex.

  1. International journal of molecular sciences · 2026
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  12. Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020
    Article
  13. Review
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  17. Carbon Catabolite Repression in Filamentous Fungi.International journal of molecular sciences · 2017
    Review
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Amparo RuizDepartment of Genetics and Development, Columbia University, New York, NY 10032, USA.
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 protein kinase of Saccharomyces cerevisiae is a member of the SNF1/AMP-activated protein kinase family, which is essential for metabolic control, energy homeostasis, and stress responses in eukaryotes. SNF1 is activated in response to glucose limitation by phosphorylation of Thr210 on the activation loop of the catalytic subunit Snf1. The SNF1 β-subunit contains a glycogen-binding domain that has been implicated in glucose inhibition of Snf1 Thr210 phosphorylation. To assess the role of glycogen, we examined Snf1 phosphorylation in strains with altered glycogen metabolism. A reg1Δ mutant, lacking Reg1-Glc7 protein phosphatase 1, exhibits elevated glycogen accumulation and phosphorylation of Snf1 during growth on high levels of glucose. Unexpectedly, mutations that abolished glycogen synthesis also restored Thr210 dephosphorylation in glucose-grown reg1Δ cells, indicating that elevated glycogen synthesis contributes to activation of SNF1 and that another phosphatase acts on Snf1. We present evidence that Sit4, a type 2A-like protein phosphatase, contributes to dephosphorylation of Snf1 Thr210. Finally, evidence that the effects of glycogen are not mediated by binding to the β-subunit raises the possibility that elevated glycogen synthesis alters glucose metabolism and thereby reduces glucose signaling to the SNF1 pathway.

Indexed as

GlucoseGlycogenMutationPhosphorylationProtein Phosphatase 1Protein Phosphatase 2Protein Serine-Threonine KinasesProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGLC7 protein, S cerevisiaeGlucoseGlycogenProtein Phosphatase 1Protein Phosphatase 2Protein Serine-Threonine KinasesREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSIT4 protein, S cerevisiaeSNF1-related protein kinases

Identifiers

PMID21464305
PMCPMC3081026
OpenAlexW2065935014

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.