Evidence map›Paper›PMID 25162638›Full record

ArticlePloS one2014

The cytosolic domain of Pex22p stimulates the Pex4p-dependent ubiquitination of the PTS1-receptor.

Fouzi El Magraoui, Andreas Schrötter, Rebecca Brinkmeier, Lena Kunst, Thomas Mastalski, Thorsten Müller, Katrin Marcus, Helmut E Meyer, Wolfgang Girzalsky, Ralf Erdmann and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. 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
1.6field-weighted citation impact, top 18% 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, 29 citations in OpenAlex.

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  5. The Structure of theFrontiers in cell and developmental biology · 2022
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  6. Non-lysine ubiquitylation: Doing things differently.Frontiers in molecular biosciences · 2022
    Review
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  8. Review
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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

11 authors at 2 institutions in 1 country.

Fouzi El MagraouiBiochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, Bochum, Germany; Systembiochemie, Ruhr-Universität Bochum, Bochum, Germany; Biomedizinische Forschung, Leibniz-Institut für Analytische Wissenschaften - ISAS -e.V., Dortmund, Germany.
Andreas SchrötterMedizinische Proteomik/Bioanalytik, AG Neuro Proteomics, Medizinisches Proteom-Center, Bochum, Germany; Biomedizinische Forschung, Leibniz-Institut für Analytische Wissenschaften - ISAS -e.V., Dortmund, Germany.
Rebecca BrinkmeierBiochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, Bochum, Germany.
Lena KunstSystembiochemie, Ruhr-Universität Bochum, Bochum, Germany.
Thomas MastalskiMedizinische Proteomik/Bioanalytik, AG Neuro Proteomics, Medizinisches Proteom-Center, Bochum, Germany.
Thorsten MüllerFunktionelle Proteomik, Medizinisches Proteom-Center, Bochum, Germany.
Katrin MarcusFunktionelle Proteomik, Medizinisches Proteom-Center, Bochum, Germany.
Helmut E MeyerBiomedizinische Forschung, Leibniz-Institut für Analytische Wissenschaften - ISAS -e.V., Dortmund, Germany.
Wolfgang GirzalskySystembiochemie, Ruhr-Universität Bochum, Bochum, Germany.
Ralf ErdmannSystembiochemie, Ruhr-Universität Bochum, Bochum, Germany.
Harald W PlattaBiochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, Bochum, Germany.
Ruhr University Bochum · DELeibniz Institute for Analytical Sciences - ISAS · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomal biogenesis is an ubiquitin-dependent process because the receptors required for the import of peroxisomal matrix proteins are controlled via their ubiquitination status. A key step is the monoubiquitination of the import receptor Pex5p by the ubiquitin-conjugating enzyme (E2) Pex4p. This monoubiquitination is supposed to take place after Pex5p has released the cargo into the peroxisomal matrix and primes Pex5p for the extraction from the membrane by the mechano-enzymes Pex1p/Pex6p. These two AAA-type ATPases export Pex5p back to the cytosol for further rounds of matrix protein import. Recently, it has been reported that the soluble Pex4p requires the interaction to its peroxisomal membrane-anchor Pex22p to display full activity. Here we demonstrate that the soluble C-terminal domain of Pex22p harbours its biological activity and that this activity is independent from its function as membrane-anchor of Pex4p. We show that Pex4p can be functionally fused to the trans-membrane segment of the membrane protein Pex3p, which is not directly involved in Pex5p-ubiquitination and matrix protein import. However, this Pex3(N)-Pex4p chimera can only complement the double-deletion strain pex4Δ/pex22Δ and ensure optimal Pex5p-ubiquitination when the C-terminal part of Pex22p is additionally expressed in the cell. Thus, while the membrane-bound portion Pex22(N)p is not required when Pex4p is fused to Pex3(N)p, the soluble Pex22(C)p is essential for peroxisomal biogenesis and efficient monoubiquitination of the import receptor Pex5p by the E3-ligase Pex12p in vivo and in vitro. The results merge into a picture of an ubiquitin-conjugating complex at the peroxisomal membrane consisting of three domains: the ubiquitin-conjugating domain (Pex4p), a membrane-anchor domain (Pex22(N)p) and an enhancing domain (Pex22(C)p), with the membrane-anchor domain being mutually exchangeable, while the Ubc- and enhancer-domains are essential.

Indexed as

Gene Expression Regulation, FungalAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesEscherichia coliGene DeletionMembrane ProteinsPeroxinsPeroxisomesPeroxisome-Targeting Signal 1 ReceptorPhosphorylationProtein Structure, TertiaryProtein TransportReceptors, Cytoplasmic and NuclearRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesMembrane ProteinsPeroxinsPeroxisome-Targeting Signal 1 ReceptorPEX1 protein, S cerevisiaePex22 protein, S cerevisiaePEX3 protein, S cerevisiaePEX4 protein, S cerevisiaePEX6 protein, S cerevisiaeReceptors, Cytoplasmic and NuclearRecombinant ProteinsSaccharomyces cerevisiae ProteinsUbiquitin

Identifiers

PMID25162638
PMCPMC4146569
OpenAlexW2055067647

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.