Evidence map›Paper›PMID 18367543›Full record

ArticleMolecular biology of the cell2008

Ear1p and Ssh4p are new adaptors of the ubiquitin ligase Rsp5p for cargo ubiquitylation and sorting at multivesicular bodies.

Sébastien Léon, Zoi Erpapazoglou, Rosine Haguenauer-Tsapis

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
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  5. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  6. Article
  7. Article
  8. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  9. Article
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  11. Article
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  17. Regulation of Krüppel-like factor 8 by the NEDD4 E3 ubiquitin ligase.American journal of translational research · 2019
    Article
  18. Article
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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

3 authors.

Sébastien LéonInstitut Jacques Monod, Unité Mixte de Recherche 7592 Centre National de la Recherche Scientifique, Universités Paris 6 et 7, 75251 Paris, France. leon@ijm.jussieu.fr
Zoi Erpapazoglou
Rosine Haguenauer-Tsapis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitylation of membrane proteins destined for the vacuole/lysosome is essential for their recognition by the endosomal sorting machinery and their internalization into vesicles of multivesicular bodies (MVBs). In yeast, this process requires Rsp5p, an essential ubiquitin ligase of the Nedd4 family. We describe here two redundant proteins, Ear1p and Ssh4p, required for the vacuolar targeting of several cargoes originating from the Golgi or the plasma membrane. Ear1p is an endosomal protein that interacts with Rsp5p through its PPxY motifs, and it is required for the ubiquitylation of selected cargoes before their MVB sorting. In-frame fusion of cargo to ubiquitin overcomes the need for Ear1p/Ssh4p, confirming a role for these proteins in cargo ubiquitylation. Interestingly, Ear1p is itself ubiquitylated by Rsp5p and targeted to the vacuole. Finally, Ear1p overexpression leads to Rsp5p accumulation at endosomes, interfering with some of its functions in trafficking. Therefore, Ear1p/Ssh4p recruit Rsp5p and assist it in its function at MVBs by directing the ubiquitylation of specific cargoes.

Indexed as

UbiquitinationAdaptor Proteins, Vesicular TransportCell MembraneEndocytosisEndosomal Sorting Complexes Required for TransportEndosomesNucleotide Transport ProteinsProtein BindingProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidUbiquitin-Protein Ligase ComplexesVacuolesAdaptor Proteins, Vesicular TransportEAR1 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportFUR4 protein, S cerevisiaeNucleotide Transport ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSSH4 protein, S cerevisiaeUbiquitin-Protein Ligase Complexes

Identifiers

PMID18367543
PMCPMC2397306

What OpenQuestion holds

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Registered trials

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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.