Evidence map›Paper›PMID 17079730›Full record

ArticleMolecular biology of the cell2007

Hse1, a component of the yeast Hrs-STAM ubiquitin-sorting complex, associates with ubiquitin peptidases and a ligase to control sorting efficiency into multivesicular bodies.

Jihui Ren, Younghoon Kee, Jon M Huibregtse, Robert C Piper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

49 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022
    Review
  5. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
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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 at 2 institutions in 1 country.

Jihui RenDepartment of Physiology and Biophysics, University of Iowa, Iowa City, IA 52242, USA.
Younghoon Kee
Jon M Huibregtse
Robert C Piper
The University of Texas at Austin · USUniversity of Iowa · US

Funding

Ubiquitin-Dependent Sorting in Endosomes and the TGNR01GM058202 · NIGMS · UNIVERSITY OF IOWA · PI PIPER, ROBERT C · 1998 to 2025
$8.9M
Specificity of Ubiquitination: the HPVE6/E6AP ParadigmR01CA072943 · NCI · UNIVERSITY OF TEXAS AUSTIN · PI HUIBREGTSE, JON · 1997 to 2011
$3.2M
NCI NIH HHS R01 CA072943NIGMS NIH HHS R01 GM058202NIGMS NIH HHS R01 GM58202
6 · The paper itself

Abstract

Ubiquitinated integral membrane proteins are delivered to the interior of the lysosome/vacuole for degradation. This process relies on specific ubiquitination of potential cargo and recognition of that Ub-cargo by sorting receptors at multiple compartments. We show that the endosomal Hse1-Vps27 sorting receptor binds to ubiquitin peptidases and the ubiquitin ligase Rsp5. Hse1 is linked to Rsp5 directly via a PY element within its C-terminus and through a novel protein Hua1, which recruits a complex of Rsp5, Rup1, and Ubp2. The SH3 domain of Hse1 also binds to the deubiquitinating protein Ubp7. Functional analysis shows that when both modes of Rsp5 association with Hse1 are altered, sorting of cargo that requires efficient ubiquitination for entry into the MVB is blocked, whereas sorting of cargo containing an in-frame addition of ubiquitin is normal. Further deletion of Ubp7 restores sorting of cargo when the Rsp5:Hse1 interaction is compromised suggesting that both ubiquitin ligases and peptidases associate with the Hse1-Vps27 sorting complex to control the ubiquitination status and sorting efficiency of cargo proteins. Additionally, we find that disruption of UBP2 and RUP1 inhibits MVB sorting of some cargos suggesting that Rsp5 requires association with Ubp2 to properly ubiquitinate cargo for efficient MVB sorting.

Indexed as

EndopeptidasesEndosomal Sorting Complexes Required for TransportMediator ComplexMultiprotein ComplexesNuclear ProteinsProtein BindingProtein Interaction MappingProtein TransportReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinssrc Homology DomainsTranscription FactorsTransport VesiclesUbiquitinEndopeptidasesEndosomal Sorting Complexes Required for TransportHse1 protein, S cerevisiaeMediator ComplexMultiprotein ComplexesNuclear ProteinsPGD1 protein, S cerevisiaeReceptors, Cytoplasmic and NuclearRecombinant Fusion ProteinsRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinubiquitin-Nalpha-protein hydrolaseUbiquitin-Protein Ligase Complexes

Identifiers

PMID17079730
PMCPMC1751313
OpenAlexW2137576392

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.