Evidence map›Paper›PMID 28552664›Full record

ArticleBiochimica et biophysica acta. Molecular cell research2017

Saccharomyces cerevisiae cells lacking Pex3 contain membrane vesicles that harbor a subset of peroxisomal membrane proteins.

Justyna P Wróblewska, Luis Daniel Cruz-Zaragoza, Wei Yuan, Andreas Schummer, Silvia G Chuartzman, Rinse de Boer, Silke Oeljeklaus, Maya Schuldiner, Einat Zalckvar, Bettina Warscheid and 2 more

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Molecular cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Peroxisomal Membrane Contact Sites in Yeasts.Frontiers in cell and developmental biology · 2021
    Review
  6. Article
  7. Review
  8. Article
  9. Frontiers in microbiology · 2019
    Article
  10. Review
  11. Review
  12. Lipid Droplet and Peroxisome Biogenesis: Do They Go Hand-in-Hand?Frontiers in cell and developmental biology · 2019
    Review
  13. Article
  14. The peroxisome: an update on mysteries 2.0.Histochemistry and cell biology · 2018
    Review
  15. 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

12 authors at 4 institutions in 3 countries.

Justyna P WróblewskaMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (BBA), University of Groningen, PO Box 11103, 9300 CC Groningen, The Netherlands.
Luis Daniel Cruz-ZaragozaSystembiochemie, Institut für Biochemie und Pathobiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, 44801 Bochum, Germany.
Wei YuanMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (BBA), University of Groningen, PO Box 11103, 9300 CC Groningen, The Netherlands.
Andreas SchummerDepartment of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.
Silvia G ChuartzmanDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Rinse de BoerMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (BBA), University of Groningen, PO Box 11103, 9300 CC Groningen, The Netherlands.
Silke OeljeklausDepartment of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany.
Maya SchuldinerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Einat ZalckvarDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot 7610001, Israel.
Bettina WarscheidDepartment of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology, University of Freiburg, 79104 Freiburg, Germany; BIOSS Centre for Biological Signalling Studies, University of Freiburg, Germany.
Ralf ErdmannSystembiochemie, Institut für Biochemie und Pathobiochemie, Medizinische Fakultät, Ruhr-Universität Bochum, 44801 Bochum, Germany. Electronic address: ralf.erdmann@rub.de.
Ida J van der KleiMolecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute (BBA), University of Groningen, PO Box 11103, 9300 CC Groningen, The Netherlands. Electronic address: i.j.van.der.klei@rug.nl.
University of Groningen · NLUniversity of Freiburg · DEWeizmann Institute of Science · ILRuhr University Bochum · DE

Funding

European Research Council 646604
6 · The paper itself

Abstract

Pex3 has been proposed to be important for the exit of peroxisomal membrane proteins (PMPs) from the ER, based on the observation that PMPs accumulate at the ER in Saccharomyces cerevisiae pex3 mutant cells. Using a combination of microscopy and biochemical approaches, we show that a subset of the PMPs, including the receptor docking protein Pex14, localizes to membrane vesicles in S. cerevisiae pex3 cells. These vesicles are morphologically distinct from the ER and do not co-sediment with ER markers in cell fractionation experiments. At the vesicles, Pex14 assembles with other peroxins (Pex13, Pex17, and Pex5) to form a complex with a composition similar to the PTS1 import pore in wild-type cells. Fluorescence microscopy studies revealed that also the PTS2 receptor Pex7, the importomer organizing peroxin Pex8, the ubiquitin conjugating enzyme Pex4 with its recruiting PMP Pex22, as well as Pex15 and Pex25 co-localize with Pex14. Other peroxins (including the RING finger complex and Pex27) did not accumulate at these structures, of which Pex11 localized to mitochondria. In line with these observations, proteomic analysis showed that in addition to the docking proteins and Pex5, also Pex7, Pex4/Pex22 and Pex25 were present in Pex14 complexes isolated from pex3 cells. However, formation of the entire importomer was not observed, most likely because Pex8 and the RING proteins were absent in the Pex14 protein complexes. Our data suggest that peroxisomal membrane vesicles can form in the absence of Pex3 and that several PMPs can insert in these vesicles in a Pex3 independent manner.

Indexed as

Arabidopsis ProteinsEndoplasmic ReticulumMembrane ProteinsMembrane Transport ProteinsPeroxinsPeroxisomesProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransport VesiclesUbiquitin-Conjugating EnzymesArabidopsis ProteinsMembrane ProteinsMembrane Transport ProteinsPeroxinsPEX14 protein, S cerevisiaePEX3 protein, S cerevisiaePEX4 protein, ArabidopsisPex8 protein, S cerevisiaeProteomeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesEndoplasmic reticulumOrganellePeroxisomal membrane proteinPeroxisomePex3Protein sortingSaccharomyces cerevisiaeYeast

Identifiers

PMID28552664
PMCPMC7611440
OpenAlexW2620390003

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.