Evidence map›Paper›PMID 10757783›Full record

ArticleMolecular and cellular biology2000

A novel cold-sensitive allele of the rate-limiting enzyme of fatty acid synthesis, acetyl coenzyme A carboxylase, affects the morphology of the yeast vacuole through acylation of Vac8p.

R Schneiter, C E Guerra, M Lampl, V Tatzer, G Zellnig, H L Klein, S D Kohlwein

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 40 citations in OpenAlex.

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  8. Genetic analysis of the Warburg effect in yeast.Advances in biological regulation · 2015
    Review
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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

7 authors at 4 institutions in 2 countries.

R SchneiterSFB Biomembrane Research Center, Institut für Biochemie und Lebensmittelchemie, Technische Universität Graz, A-8010 Graz, Austria. f548roge@mbox.tu-graz.ac.at
C E Guerra
M Lampl
V Tatzer
G Zellnig
H L Klein
S D Kohlwein
Graz University of Technology · ATColumbia University Irving Medical Center · USNew York University · USUniversity of Graz · AT

Funding

GENETIC BEHAVIOR OF REPEATED SEQUENCESR01GM030439 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI KLEIN, HANNAH L · 1985 to 2001
$739k
NIGMS NIH HHS GM30439
6 · The paper itself

Abstract

The yeast vacuole functions both as a degradative organelle and as a storage depot for small molecules and ions. Vacuoles are dynamic reticular structures that appear to alternately fuse and fragment as a function of growth stage and environment. Vac8p, an armadillo repeat-containing protein, has previously been shown to function both in vacuolar inheritance and in protein targeting from the cytoplasm to the vacuole. Both myristoylation and palmitoylation of Vac8p are required for its efficient localization to the vacuolar membrane (Y.-X. Wang, N. L. Catlett, and L. S. Weisman, J. Cell Biol. 140:1063-1074, 1998). We report that mutants with conditional defects in the rate-limiting enzyme of fatty acid synthesis, acetyl coenzyme A carboxylase (ACC1), display unusually multilobed vacuoles, similar to those observed in vac8 mutant cells. This vacuolar phenotype of acc1 mutant cells was shown biochemically to be accompanied by a reduced acylation of Vac8p which was alleviated by fatty acid supplementation. Consistent with the proposed defect of acc1 mutant cells in acylation of Vac8p, vacuolar membrane localization of Vac8p was impaired upon shifting acc1 mutant cells to nonpermissive condition. The function of Vac8p in protein targeting, on the other hand, was not affected under these conditions. These observations link fatty acid synthesis and availability to direct morphological alterations of an organellar membrane.

Indexed as

Cold TemperatureSaccharomyces cerevisiae ProteinsAcetyl-CoA CarboxylaseAcylationAllelesBlotting, WesternDNA Transposable ElementsGenetic Complementation TestLipoproteinsMembrane ProteinsMicroscopy, ElectronMicroscopy, FluorescenceMutagenesisMyristic AcidsPalmitic AcidsPhenotypeAcetyl-CoA CarboxylaseDNA Transposable ElementsLipoproteinsMembrane ProteinsMyristic AcidsPalmitic AcidsSaccharomyces cerevisiae ProteinsVAC8 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID10757783
PMCPMC85561
OpenAlexW2100785164

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.