Evidence map›Paper›PMID 27663510›Full record

ArticleJournal of cell science2016

Characterization of proteome dynamics during growth in oleate reveals a new peroxisome-targeting receptor.

Eden Yifrach, Silvia G Chuartzman, Noa Dahan, Shiran Maskit, Lior Zada, Uri Weill, Ido Yofe, Tsviya Olender, Maya Schuldiner, Einat Zalckvar

Abstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
    Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Uncovering targeting priority to yeast peroxisomes using an in-cell competition assay.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  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

10 authors at 1 institution in 1 country.

Eden YifrachDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Silvia G ChuartzmanDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Noa DahanDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Shiran MaskitDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Lior ZadaDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Uri WeillDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Ido YofeDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Tsviya OlenderDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel maya.schuldiner@weizmann.ac.il einat.zalckvar@weizmann.ac.il.ORCID 0000-0001-9947-115X
Einat ZalckvarDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel maya.schuldiner@weizmann.ac.il einat.zalckvar@weizmann.ac.il.ORCID 0000-0003-3724-3965
Weizmann Institute of Science · IL

Funding

European Research Council 646604
6 · The paper itself

Abstract

To optimally perform the diversity of metabolic functions that occur within peroxisomes, cells must dynamically regulate peroxisome size, number and content in response to the cell state and the environment. Except for transcriptional regulation little is known about the mechanisms used to perform this complicated feat. Focusing on the yeast Saccharomyces cerevisiae, we used complementary high-content screens to follow changes in localization of most proteins during growth in oleate. We found extensive changes in cellular architecture and identified several proteins that colocalized with peroxisomes that had not previously been considered peroxisomal proteins. One of the newly identified peroxisomal proteins, Ymr018w, is a protein with an unknown function that is similar to the yeast and human peroxisomal targeting receptor Pex5. We demonstrate that Ymr018w is a new peroxisomal-targeting receptor that targets a subset of matrix proteins to peroxisomes. We, therefore, renamed Ymr018w, Pex9, and suggest that Pex9 is a condition-specific targeting receptor that enables the dynamic rewiring of peroxisomes in response to metabolic needs. Moreover, we suggest that Pex5-like receptors might also exist in vertebrates.

Indexed as

Models, BiologicalOleic AcidPeroxisomesProtein TransportProteomeProteomicsReceptors, Cell SurfaceSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsOleic AcidProteomeReceptors, Cell SurfaceSaccharomyces cerevisiae ProteinsGlucoseHigh-content screenOleatePeroxisomeProtein targetingSaccharomyces cerevisiae

Identifiers

PMID27663510
PMCPMC6275125
OpenAlexW2522752792

What OpenQuestion holds

Textmetadata
LicenceTDM
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.