Evidence map›Paper›PMID 16816426›Full record

ArticleGenetics2006

The conserved ATPase Get3/Arr4 modulates the activity of membrane-associated proteins in Saccharomyces cerevisiae.

Kathryn L Auld, Amy L Hitchcock, Hugh K Doherty, Seth Frietze, Linda S Huang, Pamela A Silver

Open access · greenAbstract read
In one paragraph

Article in Genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

33 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Endoplasmic reticulum membrane receptors of the GET pathway are conserved throughout eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Mutations in the ArsA ATPase that restore interaction with the ArsD metallochaperone.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2014
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Nucleotide-dependent mechanism of Get3 as elucidated from free energy calculations.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Article
  17. Pathways of arsenic uptake and efflux.Current topics in membranes · 2012
    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

6 authors at 3 institutions in 1 country.

Kathryn L AuldDepartment of Systems Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Amy L Hitchcock
Hugh K Doherty
Seth Frietze
Linda S Huang
Pamela A Silver
Harvard University · USUniversity of Massachusetts Boston · USCenter for Systems Biology · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The regulation of cellular membrane dynamics is crucial for maintaining proper cell growth and division. The Cdc48-Npl4-Ufd1 complex is required for several regulated membrane-associated processes as part of the ubiquitin-proteasome system, including ER-associated degradation and the control of lipid composition in yeast. In this study we report the results of a genetic screen in Saccharomyces cerevisiae for extragenic suppressors of a temperature-sensitive npl4 allele and the subsequent analysis of one suppressor, GET3/ARR4. The GET3 gene encodes an ATPase with homology to the regulatory component of the bacterial arsenic pump. Mutants of GET3 rescue several phenotypes of the npl4 mutant and transcription of GET3 is coregulated with the proteasome, illustrating a functional relationship between GET3 and NPL4 in the ubiquitin-proteasome system. We have further found that Get3 biochemically interacts with the trans-membrane domain proteins Get1/Mdm39 and Get2/Rmd7 and that Deltaget3 is able to suppress phenotypes of get1 and get2 mutants, including sporulation defects. In combination, our characterization of GET3 genetic and biochemical interactions with NPL4, GET1, and GET2 implicates Get3 in multiple membrane-dependent pathways.

Indexed as

Adaptor Proteins, Vesicular TransportAdenosine TriphosphatasesArabidopsis ProteinsCell Cycle ProteinsGene Expression Regulation, FungalMembrane ProteinsMultiprotein ComplexesMutationNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsPhenotypeProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpores, FungalSuppression, GeneticAdaptor Proteins, Vesicular TransportAdenosine TriphosphatasesArabidopsis ProteinsARR4 protein, ArabidopsisCDC48 protein, S cerevisiaeCell Cycle ProteinsGET1 protein, S cerevisiaeGet2 protein, S cerevisiaeMembrane ProteinsMultiprotein ComplexesNPL4 protein, S cerevisiaeNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsUFD1 protein, S cerevisiaeValosin Containing ProteinVesicular Transport Proteins

Identifiers

PMID16816426
PMCPMC1569774
OpenAlexW2073231769

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.