Evidence map›Paper›PMID 16363994›Full record

ArticleThe Biochemical journal2006

Enhanced levels of Pis1p (phosphatidylinositol synthase) improve the growth of Saccharomyces cerevisiae cells deficient in Rsp5 ubiquitin ligase.

Pawel Kaliszewski, Thierry Ferreira, Beata Gajewska, Anna Szkopinska, Thierry Berges, Teresa Zoładek

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

10 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  10. Functional dissection of a HECT ubiquitin E3 ligase.Molecular & cellular proteomics : MCP · 2008
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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

6 authors at 3 institutions in 2 countries.

Pawel KaliszewskiDepartment of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
Thierry Ferreira
Beata Gajewska
Anna Szkopinska
Thierry Berges
Teresa Zoładek
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PLCentre National de la Recherche Scientifique · FRMedical University of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rsp5 ubiquitin ligase plays a role in many cellular processes including the biosynthesis of unsaturated fatty acids. The PIS1 (phosphatidylinositol synthase gene) encoding the enzyme Pis1p which catalyses the synthesis of phosphatidylinositol from CDP-diacyglycerol and inositol, was isolated in a screen for multicopy suppressors of the rsp5 temperature sensitivity phenotype. Suppression was allele non-specific. Interestingly, expression of PIS1 was 2-fold higher in the rsp5 mutant than in wild-type yeast, whereas the introduction of PIS1 in a multicopy plasmid increased the level of Pis1p 6-fold in both backgrounds. We demonstrate concomitantly that the expression of INO1 (inositol phosphate synthase gene) was also elevated approx. 2-fold in the rsp5 mutant as compared with the wild-type, and that inositol added to the medium improved growth of rsp5 mutants at a restrictive temperature. These results suggest that enhanced phosphatidylinositol synthesis may account for PIS1 suppression of rsp5 defects. Analysis of lipid extracts revealed the accumulation of saturated fatty acids in the rsp5 mutant, as a consequence of the prevention of unsaturated fatty acid synthesis. Overexpression of PIS1 did not correct the cellular fatty acid content; however, saturated fatty acids (C(16:0)) accumulated preferentially in phosphatidylinositol, and (wild-type)-like fatty acid composition in phosphatidylethanolamine was restored.

Indexed as

CatalysisCell SurvivalEndosomal Sorting Complexes Required for TransportFatty AcidsGene Expression Regulation, FungalGenes, SuppressorInositolMutationMyo-Inositol-1-Phosphate SynthasePhenotypePhosphatidylethanolaminesPhosphatidylinositolsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTemperatureTransferases (Other Substituted Phosphate Groups)Endosomal Sorting Complexes Required for TransportFatty AcidsInositolMyo-Inositol-1-Phosphate SynthasephosphatidylethanolaminePhosphatidylethanolaminesPhosphatidylinositolsPIS1 protein, S cerevisiaeRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTransferases (Other Substituted Phosphate Groups)Ubiquitin-Protein Ligase Complexes

Identifiers

PMID16363994
PMCPMC1409703
OpenAlexW2094609327

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.