Evidence map›Paper›PMID 17145966›Full record

ArticleThe Journal of cell biology2006

A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function.

Alexander Amerik, Nazia Sindhi, Mark Hochstrasser

Abstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Genetic Selection Based on a Ste6G3 (Bethesda, Md.) · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Ubiquitin-dependent sorting in endocytosis.Cold Spring Harbor perspectives in biology · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. How ubiquitin functions with ESCRTs.Traffic (Copenhagen, Denmark) · 2011
    Review
  17. Structural basis for ESCRT-III CHMP3 recruitment of AMSH.Structure (London, England : 1993) · 2011
    Article
  18. Review
  19. Article
  20. Article
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

3 authors.

Alexander AmerikDepartment of Pharmacology, University of Connecticut Health Center, Farmington, CT 06030, USA. amerik@uchc.edu
Nazia Sindhi
Mark Hochstrasser

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

Enzyme specificity in vivo is often controlled by subcellular localization. Yeast Doa4, a deubiquitylating enzyme (DUB), removes ubiquitin from membrane proteins destined for vacuolar degradation. Doa4 is recruited to the late endosome after ESCRT-III (endosomal sorting complex required for transport III) has assembled there. We show that an N-terminal segment of Doa4 is sufficient for endosome association. This domain bears four conserved elements (boxes A-D). Deletion of the most conserved of these, A or B, prevents Doa4 endosomal localization. These mutants cannot sustain ubiquitin-dependent proteolysis even though neither motif is essential for deubiquitylating activity. Ubiquitin-specific processing protease 5 (Ubp5), the closest paralogue of Doa4, has no functional overlap. Ubp5 concentrates at the bud neck; its N-terminal domain is critical for this. Importantly, substitution of the Ubp5 N-terminal domain with that of Doa4 relocalizes the Ubp5 enzyme to endosomes and provides Doa4 function. This is the first demonstration of a physiologically important DUB subcellular localization signal and provides a striking example of the functional diversification of DUB paralogues by the evolution of alternative spatial signals.

Indexed as

Protein Sorting SignalsAmino Acid SequenceConserved SequenceEndopeptidasesEndosomal Sorting Complexes Required for TransportEndosomesIntracellular MembranesMolecular Sequence DataPhenotypeProtein Structure, TertiaryProtein TransportSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitinUbiquitin ThiolesteraseVesicular Transport ProteinsBro1 protein, S cerevisiaeDOA4 protein, S cerevisiaeEndopeptidasesEndosomal Sorting Complexes Required for TransportProtein Sorting SignalsSaccharomyces cerevisiae ProteinsUbiquitinUbiquitin ThiolesteraseVesicular Transport Proteins

Identifiers

PMID17145966
PMCPMC2064681

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.