Evidence map›Paper›PMID 23689284›Full record

ArticleMolecular & cellular proteomics : MCP2013

A combined approach of quantitative interaction proteomics and live-cell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesis.

Christine David, Johannes Koch, Silke Oeljeklaus, Alexandra Laernsack, Sophie Melchior, Sebastian Wiese, Andreas Schummer, Ralf Erdmann, Bettina Warscheid, Cécile Brocard

Abstract read
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Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

53 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

10 authors.

Christine DavidUniversity of Vienna, Max F. Perutz Laboratories, Center of Molecular Biology, Department of Biochemistry and Cell Biology, Dr. Bohr-Gasse 9, A-1030, Vienna, Austria.
Johannes Koch
Silke Oeljeklaus
Alexandra Laernsack
Sophie Melchior
Sebastian Wiese
Andreas Schummer
Ralf Erdmann
Bettina Warscheid
Cécile Brocard

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisome biogenesis initiates at the endoplasmic reticulum (ER) and maturation allows for the formation of metabolically active organelles. Yet, peroxisomes can also multiply by growth and division. Several proteins, called peroxins, are known to participate in these processes but little is known about their organization to orchestrate peroxisome proliferation. Here, we demonstrate that regulation of peroxisome proliferation relies on the integrity of the tubular ER network. Using a dual track SILAC-based quantitative interaction proteomics approach, we established a comprehensive network of stable as well as transient interactions of the peroxin Pex30p, an integral membrane protein. Through association with merely ER resident proteins, in particular with proteins containing a reticulon homology domain, and with other peroxins, Pex30p designates peroxisome contact sites at ER subdomains. We show that Pex30p traffics through the ER and segregates in punctae to which peroxisomes specifically append, and we ascertain its transient interaction with all subunits of the COPI coatomer complex suggesting the involvement of a vesicle-mediated transport. We establish that the membrane protein Pex30p facilitates the connection of peroxisomes to the ER. Taken together, our data indicate that Pex30p-containing protein complexes act as focal points from which peroxisomes can form and that the tubular ER architecture organized by the reticulon homology proteins Rtn1p, Rtn2p and Yop1p controls this process.

Indexed as

Imaging, Three-DimensionalSequence Homology, Amino AcidCell NucleusCoatomer ProteinDiffusionEndoplasmic ReticulumHumansIsotope LabelingMass SpectrometryMembrane ProteinsPeroxisomesProtein BindingProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCoatomer ProteinMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID23689284
PMCPMC3769320

What OpenQuestion holds

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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.