Evidence map›Paper›PMID 15456873›Full record

ArticleMolecular and cellular biology2004

Regulation and recognition of SCFGrr1 targets in the glucose and amino acid signaling pathways.

Nathalie Spielewoy, Karin Flick, Tatyana I Kalashnikova, John R Walker, Curt Wittenberg

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

53 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. Article
  7. Regulation ofmBio · 2018
    Article
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  9. Article
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  11. Review
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  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. SUMOylation regulates the SNF1 protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

5 authors at 3 institutions in 1 country.

Nathalie SpielewoyDepartment of Molecular Biology, MB-3, The Scripps Research Institute, 10550 North Torrey Pines Rd., La Jolla, CA 92037, USA.
Karin Flick
Tatyana I Kalashnikova
John R Walker
Curt Wittenberg
Scripps Research Institute · USGenomics Institute of the Novartis Research Foundation · USUniversity of California, Irvine · US

Funding

REGULATION OF G1-SPECIFIC GENE EXPRESSION IN YEASTR01GM059441 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI WITTENBERG, CURT · 2000 to 2016
$6.9M
ROLE OF CYCLINS IN CONTROL OF THE YEAST CELL CYCLER01GM043487 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI WITTENBERG, CURT · 1990 to 2005
$2.0M
NIGMS NIH HHS GM43487NIGMS NIH HHS GM59441NIGMS NIH HHS R01 GM043487NIGMS NIH HHS R01 GM059441
6 · The paper itself

Abstract

SCFGrr1, one of several members of the SCF family of E3 ubiquitin ligases in budding Saccharomyces cerevisiae, is required for both regulation of the cell cycle and nutritionally controlled transcription. In addition to its role in degradation of Gic2 and the CDK targets Cln1 and Cln2, Grr1 is also required for induction of glucose- and amino acid-regulated genes. Induction of HXT genes by glucose requires the Grr1-dependent degradation of Mth1. We show that Mth1 is ubiquitinated in vivo and degraded via the proteasome. Furthermore, phosphorylated Mth1, targeted by the casein kinases Yck1/2, binds to Grr1. That binding depends upon the Grr1 leucine-rich repeat (LRR) domain but not upon the F-box or basic residues within the LRR that are required for recognition of Cln2 and Gic2. Those observations extend to a large number of Grr1-dependent genes, some targets of the amino acid-regulated SPS signaling system, which are properly regulated in the absence of those basic LRR residues. Finally, we show that regulation of the SPS targets requires the Yck1/2 casein kinases. We propose that casein kinase I plays a similar role in both nutritional signaling pathways by phosphorylating pathway components and targeting them for ubiquitination by SCFGrr1.

Indexed as

Gene Expression Regulation, FungalAdaptor Proteins, Signal TransducingAmino AcidsCasein Kinase ICyclinsF-Box ProteinsGlucoseGlucose Transport Proteins, FacilitativeMembrane ProteinsMonosaccharide Transport ProteinsMutationProteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingAmino AcidsCasein Kinase ICLN2 protein, S cerevisiaeCyclinsF-Box ProteinsGlucoseGlucose Transport Proteins, FacilitativeGRR1 protein, S cerevisiaeHXT3 protein, S cerevisiaeMembrane ProteinsMonosaccharide Transport ProteinsMTH1 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSKP1 protein, S cerevisiaeSKP Cullin F-Box Protein LigasesUbiquitinUbiquitin-Protein LigasesYCK1 protein, S cerevisiae

Identifiers

PMID15456873
PMCPMC517892
OpenAlexW2143395036

What OpenQuestion holds

Textmetadata
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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.