Evidence map›Paper›PMID 11416128›Full record

ArticleMolecular and cellular biology2001

Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase.

S Dupré, R Haguenauer-Tsapis

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

67 citing papers in PubMed, 155 citations in OpenAlex.

  1. Article
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  7. Life and Death of Fungal Transporters under the Challenge of Polarity.International journal of molecular sciences · 2020
    Review
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  14. Deubiquitinase Usp8 regulates α-synuclein clearance and modifies its toxicity in Lewy body disease.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Review
  17. Article
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  19. Review
  20. Article

7 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

S DupréInstitut Jacques Monod-CNRS, Université Paris VII, 75005 Paris, France.
R Haguenauer-Tsapis
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Fur4p uracil permease, like most yeast plasma membrane proteins, undergoes ubiquitin-dependent endocytosis and is then targeted to the vacuole (equivalent to the mammalian lysosome) for degradation. The cell surface ubiquitination of Fur4p is mediated by the essential Rsp5p ubiquitin ligase. Ubiquitination of Fur4p occurs on two target lysines, which receive two ubiquitin moieties linked through ubiquitin Lys63, a type of linkage (termed UbK63) different from that involved in proteasome recognition. We report that pep4 cells deficient for vacuolar protease activities accumulate vacuolar unubiquitinated Fur4p. In contrast, pep4 cells lacking the Doa4p ubiquitin isopeptidase accumulate ubiquitin-conjugated Fur4p. These data suggest that Fur4p undergoes Doa4p-dependent deubiquitination prior to vacuolar degradation. Compared to pep4 cells, pep4 doa4 cells have huge amounts of membrane-bound ubiquitin conjugates. This indicates that Doa4p plays a general role in the deubiquitination of membrane-bound proteins, as suggested by reports describing the suppression of some doa4 phenotypes in endocytosis and vacuolar protein sorting mutants. Some of the small ubiquitin-linked peptides that are a hallmark of Doa4 deficiency are not present in rsp5 mutant cells or after overproduction of a variant ubiquitin modified at Lys 63 (UbK63R). These data suggest that the corresponding peptides are degradation products of Rsp5p substrates and probably of ubiquitin conjugates carrying UbK63 linkages. Doa4p thus appears to be involved in the deubiquitination of endocytosed plasma membrane proteins, some of them carrying UbK63 linkages.

Indexed as

Nucleotide Transport ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesVesicular Transport ProteinsCarrier ProteinsEndocytosisEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsLigasesMembrane ProteinsMembrane Transport ProteinsPeptidesSaccharomyces cerevisiaeUbiquitin-Protein LigasesUbiquitinsCarrier ProteinsDOA4 protein, S cerevisiaeEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsFUR4 protein, S cerevisiaeLigasesMembrane ProteinsMembrane Transport ProteinsNucleotide Transport ProteinsPeptidesRSP5 protein, S cerevisiaeSaccharomyces cerevisiae Proteinsubiquitin isopeptidaseUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbiquitinsUbiquitin ThiolesteraseVesicular Transport ProteinsVPS27 protein, S cerevisiae

Identifiers

PMID11416128
PMCPMC87108
OpenAlexW2089340389

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.