Evidence map›Paper›PMID 11029042›Full record

ArticleMolecular biology of the cell2000

The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways.

A Y Amerik, J Nowak, S Swaminathan, M Hochstrasser

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

121 citing papers in PubMed, 297 citations in OpenAlex.

  1. Trial
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  7. Genetic Selection Based on a Ste6G3 (Bethesda, Md.) · 2020
    Article
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  10. The many functions of ESCRTs.Nature reviews. Molecular cell biology · 2020
    Review
  11. Review
  12. Article
  13. Article
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  15. Review
  16. Article
  17. ESCRT-dependent cargo sorting at multivesicular endosomes.Seminars in cell & developmental biology · 2018
    Review
  18. Article
  19. Article
  20. Article

61 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

4 authors at 2 institutions in 1 country.

A Y AmerikDepartment of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520, USA.
J Nowak
S Swaminathan
M Hochstrasser
University of Chicago · USYale University · US

Funding

FUNCTIONS AND MECHANISMS OF DEUBIQUITINATING ENZYMESR01GM053756 · NIGMS · YALE UNIVERSITY · PI HOCHSTRASSER, MARK W · 1996 to 2019
$6.5M
NIGMS NIH HHS GM53756NIGMS NIH HHS R01 GM053756
6 · The paper itself

Abstract

The Saccharomyces cerevisiae DOA4 gene encodes a deubiquitinating enzyme that is required for rapid degradation of ubiquitin-proteasome pathway substrates. Both genetic and biochemical data suggest that Doa4 acts in this pathway by facilitating ubiquitin recycling from ubiquitinated intermediates targeted to the proteasome. Here we describe the isolation of 12 spontaneous extragenic suppressors of the doa4-1 mutation; these involve seven different genes, six of which were cloned. Surprisingly, all of the cloned DID (Doa4-independent degradation) genes encode components of the vacuolar protein-sorting (Vps) pathway. In particular, all are class E Vps factors, which function in the maturation of a late endosome/prevacuolar compartment into multivesicular bodies that then fuse with the vacuole. Four of the six Did proteins are structurally related, suggesting an overlap in function. In wild-type and several vps strains, Doa4-green fluorescent protein displays a cytoplasmic/nuclear distribution. However, in cells lacking the Vps4/Did6 ATPase, a large fraction of Doa4-green fluorescent protein, like several other Vps factors, concentrates at the late endosome-like class E compartment adjacent to the vacuole. These results suggest an unanticipated connection between protein deubiquitination and endomembrane protein trafficking in which Doa4 acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole.

Indexed as

EndopeptidasesSaccharomyces cerevisiae ProteinsAdenocarcinomaAmino Acid SequenceBreast NeoplasmsCysteine EndopeptidasesEndocytosisEndosomal Sorting Complexes Required for TransportFemaleFungal ProteinsGenotypeHumansMolecular Sequence DataMultienzyme ComplexesMutagenesisProteasome Endopeptidase ComplexCysteine EndopeptidasesDOA4 protein, S cerevisiaeEndopeptidasesEndosomal Sorting Complexes Required for TransportFungal ProteinsMultienzyme ComplexesProteasome Endopeptidase ComplexRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitinsUbiquitin Thiolesterase

Identifiers

PMID11029042
PMCPMC14998
OpenAlexW2140408658

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.