Evidence map›Paper›PMID 9475719›Full record

ArticleGenetics1998

An essential function of a phosphoinositide-specific phospholipase C is relieved by inhibition of a cyclin-dependent protein kinase in the yeast Saccharomyces cerevisiae.

J S Flick, J Thorner

Abstract read
In one paragraph

Article in Genetics, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 55 citations in OpenAlex.

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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

2 authors at 2 institutions in 1 country.

J S FlickDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146, USA. flickjs@ctrvax.vanderbilt.edu
J Thorner
University of California, Berkeley · USVanderbilt University · US

Funding

Yeast Protein Kinase Signaling Networks: Specificity, Regulation and FunctionR01GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1985 to 2019
$11.8M
YEAST PEPTIDE HORMONE SYNTHESIS AND SIGNAL TRANSDUCTIONR37GM021841 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI THORNER, JEREMY W. · 1989 to 1998
–
NIGMS NIH HHS GM21841
6 · The paper itself

Abstract

The PLC1 gene product of Saccharomyces cerevisiae is a homolog of the delta isoform of mammalian phosphoinositide-specific phospholipase C (PI-PLC). We found that two genes (SPL1 and SPL2), when overexpressed, can bypass the temperature-sensitive growth defect of a plc1delta cell. SPL1 is identical to the PHO81 gene, which encodes an inhibitor of a cyclin (Pho80p)-dependent protein kinase (Pho85p) complex (Cdk). In addition to overproduction of Pho81p, two other conditions that inactivate this Cdk, a cyclin (pho80delta) mutation and growth on low-phosphate medium, also permitted growth of plc1delta cells at the restrictive temperature. Suppression of the temperature sensitivity of plc1delta cells by pho80delta does not depend upon the Pho4p transcriptional regulator, the only known substrate of the Pho80p/Pho85p Cdk. The second suppressor, SPL2, encodes a small (17-kD) protein that bears similarity to the ankyrin repeat regions present in Pho81p and in other known Cdk inhibitors. Both pho81delta and spl2delta show a synthetic phenotype in combination with plc1delta. Unlike single mutants, plc1delta pho81delta and plc1delta spl2delta double mutants were unable to grow on synthetic complete medium, but were able to grow on rich medium.

Indexed as

Enzyme InhibitorsGene Expression Regulation, FungalProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceBase SequenceCyclin-Dependent Kinase Inhibitor ProteinsCyclin-Dependent KinasesCyclinsDeoxyribodipyrimidine Photo-LyaseEnzyme RepressionEpistasis, GeneticFungal ProteinsGenes, FungalMolecular Sequence DataCyclin-Dependent Kinase Inhibitor ProteinsCyclin-Dependent KinasesCyclinsDeoxyribodipyrimidine Photo-LyaseEnzyme InhibitorsFungal ProteinsPHO80 protein, S cerevisiaePHO81 protein, S cerevisiaePhosphatesPhosphatidylinositol Diacylglycerol-LyasePhosphoinositide Phospholipase CProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSPL2 protein, S cerevisiaespore photoproduct lyaseType C Phospholipases

Identifiers

PMID9475719
PMCPMC1459775
OpenAlexW2147776172

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.