Evidence map›Paper›PMID 11294906›Full record

ArticleMolecular biology of the cell2001

Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 Mutant.

S Losko, F Kopp, A Kranz, R Kölling

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

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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.

S LoskoInstitut für Mikrobiologie, Heinrich-Heine-Universität Düsseldorf, D-40225 Düsseldorf, Germany.
F Kopp
A Kranz
R Kölling

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous experiments suggested that trafficking of the a-factor transporter Ste6 of Saccharomyces cerevisiae to the yeast vacuole is regulated by ubiquitination. To define the ubiquitination-dependent step in the trafficking pathway, we examined the intracellular localization of Ste6 in the ubiquitination-deficient doa4 mutant by immunofluorescence experiments, with a Ste6-green fluorescent protein fusion protein and by sucrose density gradient fractionation. We found that Ste6 accumulated at the vacuolar membrane in the doa4 mutant and not at the cell surface. Experiments with a doa4 pep4 double mutant showed that Ste6 uptake into the lumen of the vacuole is inhibited in the doa4 mutant. The uptake defect could be suppressed by expression of additional ubiquitin, indicating that it is primarily the result of a lowered ubiquitin level (and thus of reduced ubiquitination) and not the result of a deubiquitination defect. Based on our findings, we propose that ubiquitination of Ste6 or of a trafficking factor is required for Ste6 sorting into the multivesicular bodies pathway. In addition, we obtained evidence suggesting that Ste6 recycles between an internal compartment and the plasma membrane.

Indexed as

GlycoproteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsATP-Binding Cassette TransportersBiological TransportCell MembraneEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsIntracellular MembranesMunc18 ProteinsMutagenesisNerve Tissue ProteinsSaccharomyces cerevisiaeUbiquitinsUbiquitin ThiolesteraseATP-Binding Cassette TransportersDOA4 protein, S cerevisiaeEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsGlycoproteinsMunc18 ProteinsNerve Tissue ProteinsSaccharomyces cerevisiae ProteinsSEC1 protein, S cerevisiaeSTE6 protein, S cerevisiaeUbiquitinsUbiquitin ThiolesteraseVesicular Transport Proteins

Identifiers

PMID11294906
PMCPMC32286

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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.