Evidence map›Paper›PMID 30361468›Full record

ArticleThe Journal of cell biology2019

Rsp5 Ubiquitin ligase-mediated quality control system clears membrane proteins mistargeted to the vacuole membrane.

Richa Sardana, Lu Zhu, Scott D Emr

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

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  11. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  12. Article
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  14. Article
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  16. Article
  17. Protein quality control in the secretory pathway.The Journal of cell biology · 2019
    Review
  18. Article
  19. 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 at 1 institution in 1 country.

Richa SardanaDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY.
Lu ZhuDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY.ORCID 0000-0001-9438-9296
Scott D EmrDepartment of Molecular Biology and Genetics, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY sde26@cornell.edu.ORCID 0000-0002-5408-6781
Cornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Maintenance of organelle identity is profoundly dependent on the coordination between correct targeting of proteins and removal of mistargeted and damaged proteins. This task is mediated by organelle-specific protein quality control (QC) systems. In yeast, the endocytosis and QC of most plasma membrane (PM) proteins requires the Rsp5 ubiquitin ligase and ART adaptor network. We show that intracellular adaptors of Rsp5, Ear1, and Ssh4 mediate recognition and vacuolar degradation of PM proteins that escape or bypass PM QC systems. This second tier of surveillance helps to maintain cell integrity upon heat stress and protects from proteotoxicity. To understand the mechanism of the recognition of aberrant PM cargos by Ssh4-Rsp5, we mistarget multiple PM proteins de novo to the vacuolar membrane. We found that Ssh4-Rsp5 can target and ubiquitinate multiple lysines within a restricted distance from the membrane, providing a fail-safe mechanism for a diverse cargo repertoire. The mistargeting or misfolding of PM proteins likely exposes these lysines or shifts them into the "ubiquitination zone" accessible to the Ssh4-Rsp5 complex.

Indexed as

Gene Expression Regulation, FungalActin-Related Protein 2-3 ComplexAdaptor Proteins, Vesicular TransportAmino Acid SequenceCell MembraneEndocytosisEndosomal Sorting Complexes Required for TransportHot TemperatureIntracellular MembranesLysineProtein TransportProteolysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSignal TransductionStress, PhysiologicalActin-Related Protein 2-3 ComplexAdaptor Proteins, Vesicular TransportEAR1 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportLysineRSP5 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSSH4 protein, S cerevisiaeUbiquitin-Protein Ligase Complexes

Identifiers

PMID30361468
PMCPMC6314561
OpenAlexW2898595022

What OpenQuestion holds

Textmetadata
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.