Evidence map›Paper›PMID 10990457›Full record

ArticleThe EMBO journal2000

beta-subunits of Snf1 kinase are required for kinase function and substrate definition.

M C Schmidt, R R McCartney

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

96 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
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  7. Review
  8. Advances inJournal of fungi (Basel, Switzerland) · 2023
    Review
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  14. Characterization of3 Biotech · 2021
    Article
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  20. Fine-Tuning of Energy Levels RegulatesFrontiers in physiology · 2020
    Article

36 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

2 authors at 1 institution in 1 country.

M C SchmidtDepartment of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA. mcs2@pitt.edu
R R McCartney
University of Pittsburgh · US

Funding

MECHANISMS OF GLUCOSE SIGNAL TRANSDUCTION IN YEASTR01GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1995 to 2021
$7.1M
DNA BINDING OF RECOMBINANT TFII D PROTEINSR29GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1991 to 1994
–
NIGMS NIH HHS GM46443NIGMS NIH HHS R01 GM046443
6 · The paper itself

Abstract

The Snf1 kinase and its mammalian homolog, the AMP-activated protein kinase, are heterotrimeric enzymes composed of a catalytic alpha-subunit, a regulatory gamma-subunit and a beta-subunit that mediates heterotrimer formation. Saccharomyces cerevisiae encodes three beta-subunit genes, SIP1, SIP2 and GAL83. Earlier studies suggested that these subunits may not be required for Snf1 kinase function. We show here that complete and precise deletion of all three beta-subunit genes inactivates the Snf1 kinase. The sip1Delta sip2Delta gal83Delta strain is unable to derepress invertase, grows poorly on alternative carbon sources and fails to direct the phosphorylation of the Mig1 and Sip4 proteins in vivo. The SIP1 sip2Delta gal83Delta strain manifests a subset of Snf phenotypes (Raf(+), Gly(-)) observed in the snf1Delta 10 strain (Raf(-), Gly(-)), suggesting that individual beta-subunits direct the Snf1 kinase to a subset of its targets in vivo. Indeed, deletion of individual beta-subunit genes causes distinct differences in the induction and phosphorylation of Sip4, strongly suggesting that the beta-subunits play an important role in substrate definition.

Indexed as

Saccharomyces cerevisiae ProteinsAMP-Activated Protein KinasesBasic-Leucine Zipper Transcription Factorsbeta-FructofuranosidaseBlotting, WesternCell DivisionDNA-Binding ProteinsEpitopesFungal ProteinsGene DeletionGenetic Complementation TestGlucoseGlycoside HydrolasesModels, BiologicalMutagenesis, Site-DirectedPhenotypeAMP-Activated Protein KinasesBasic-Leucine Zipper Transcription Factorsbeta-FructofuranosidaseDNA-Binding ProteinsEpitopesFungal ProteinsGlucoseGlycoside HydrolasesMIG1 protein, S cerevisiaeProtein Serine-Threonine KinasesRepressor ProteinsSaccharomyces cerevisiae ProteinsSIP1 protein, S cerevisiaeSIP4 protein, S cerevisiaeSNF1-related protein kinasesTrans-Activators

Identifiers

PMID10990457
PMCPMC314222
OpenAlexW2073068696

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.