Evidence map›Paper›PMID 20170726›Full record

ArticleCellular signalling2010

PP1 phosphatase-binding motif in Reg1 protein of Saccharomyces cerevisiae is required for interaction with both the PP1 phosphatase Glc7 and the Snf1 protein kinase.

Shadi Tabba, Simmanjeet Mangat, Rhonda McCartney, Martin C Schmidt

Abstract read
In one paragraph

Article in Cellular signalling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

16 citing papers in PubMed, 28 citations in OpenAlex.

  1. Glucose repression ofbioRxiv : the preprint server for biology · 2026
    Article
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  6. Article
  7. Carbon Catabolite Repression in Filamentous Fungi.International journal of molecular sciences · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
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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.

Shadi TabbaDivision of Pediatric Endocrinology, Children's Hospital of Pittsburgh, PA, USA.
Simmanjeet Mangat
Rhonda McCartney
Martin C Schmidt
University of Pittsburgh · US

Funding

University of Pittsburgh Clinical and Translational Science InstituteUL1TR000005 · NCATS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI REIS, STEVEN E · 2012 to 2015
$50.8M
MECHANISMS OF GLUCOSE SIGNAL TRANSDUCTION IN YEASTR01GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1995 to 2021
$7.1M
RESEARCH TRAINING IN PEDIATRIC ENDOCRINOLOGY &DIABETEST32DK007729 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MUZUMDAR, RADHIKA HIREN · 1995 to 2020
$3.3M
DNA BINDING OF RECOMBINANT TFII D PROTEINSR29GM046443 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SCHMIDT, MARTIN C · 1991 to 1994
–
NCATS NIH HHS UL1 TR000005NIDDK NIH HHS DK007729NIDDK NIH HHS T32 DK007729NIGMS NIH HHS GM46443NIGMS NIH HHS R01 GM046443
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, Snf1 kinase, the ortholog of the mammalian AMP-activated protein kinase, is activated by an increase in the phosphorylation of the conserved threonine residue in its activation loop. The phosphorylation status of this key site is determined by changes in the rate of dephosphorylation catalyzed by the yeast PP1 phosphatase Glc7 in a complex with the Reg1 protein. Reg1 and many PP1 phosphatase regulatory subunits utilize some variation of the conserved RVxF motif for interaction with PP1. In the Snf1 pathway, the exact role of the Reg1 protein is uncertain since it binds to both the Glc7 phosphatase and to Snf1, the Glc7 substrate. In this study we sought to clarify the role of Reg1 by separating the Snf1- and Glc7-binding functions. We generated a series of Reg1 proteins, some with deletions of conserved domains and one with two amino acid changes in the RVxF motif. The ability of Reg1 to bind Snf1 and Glc7 required the same domains of Reg1. Further, the RVxF motif that is essential for Reg1 binding to Glc7 is also required for binding to Snf1. Our data suggest that the regulation of Snf1 dephosphorylation is imparted through a dynamic competition between the Glc7 phosphatase and the Snf1 kinase for binding to the PP1 regulatory subunit Reg1.

Indexed as

Amino Acid Motifsbeta-FructofuranosidaseMutationProtein Interaction Domains and MotifsProtein Phosphatase 1Protein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsbeta-FructofuranosidaseGLC7 protein, S cerevisiaeProtein Phosphatase 1Protein Serine-Threonine KinasesREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF1-related protein kinasesSUC2 protein, S cerevisiae

Identifiers

PMID20170726
PMCPMC2860547
OpenAlexW2014852242

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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.