Evidence map›Paper›PMID 18474591›Full record

ArticleThe Journal of biological chemistry2008

Roles of the glycogen-binding domain and Snf4 in glucose inhibition of SNF1 protein kinase.

Milica Momcilovic, Surtaj H Iram, Yang Liu, Marian Carlson

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Advances inJournal of fungi (Basel, Switzerland) · 2023
    Review
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  15. Review
  16. Heterotrimer-independent regulation of activation-loop phosphorylation of Snf1 protein kinase involves two protein phosphatases.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Article
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  19. Roles of two protein phosphatases, Reg1-Glc7 and Sit4, and glycogen synthesis in regulation of SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

4 authors at 1 institution in 1 country.

Milica MomcilovicDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA.
Surtaj H Iram
Yang Liu
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 GM034095
6 · The paper itself

Abstract

The SNF1/AMP-activated protein kinase (AMPK) family is required for adaptation to metabolic stress and energy homeostasis. The gamma subunit of AMPK binds AMP and ATP, and mutations that affect binding cause human disease. We have here addressed the role of the Snf4 (gamma) subunit in regulating SNF1 protein kinase in response to glucose availability in Saccharomyces cerevisiae. Previous studies of mutant cells lacking Snf4 suggested that Snf4 counteracts autoinhibition by the C-terminal sequence of the Snf1 catalytic subunit but is dispensable for glucose regulation, and AMP does not activate SNF1 in vitro. We first introduced substitutions at sites that, in AMPK, contribute to nucleotide binding and regulation. Mutations at several sites relieved glucose inhibition of SNF1, as judged by catalytic activity, phosphorylation of the activation-loop Thr-210, and growth assays, although analogs of the severe human mutations R531G/Q had little effect. We further showed that alterations of Snf4 residues that interact with the glycogen-binding domain (GBD) of the beta subunit strongly relieved glucose inhibition. Finally, substitutions in the GBD of the Gal83 beta subunit that are predicted to disrupt interactions with Snf4 and also complete deletion of the GBD similarly relieved glucose inhibition of SNF1. Analysis of mutant cells lacking glycogen synthase showed that regulation of SNF1 is normal in the absence of glycogen. These findings reveal novel roles for Snf4 and the GBD in regulation of SNF1.

Indexed as

Amino Acid SubstitutionAMP-Activated Protein KinasesCarrier ProteinsCatalytic DomainEnergy MetabolismGlucoseGlycogenGlycogen SynthaseHumansMultienzyme ComplexesMutationPhosphorylationProtein Serine-Threonine KinasesProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeAMP-Activated Protein KinasesCarrier ProteinsGlucoseGlycogenGlycogen SynthaseMultienzyme ComplexesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesSNF4 protein, S cerevisiaeTranscription Factors

Identifiers

PMID18474591
PMCPMC2443652
OpenAlexW2080647804

What OpenQuestion holds

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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.