Evidence map›Paper›PMID 40344504›Full record

ArticleThe FEBS journal2025

Msp1 and Pex19-Pex3 cooperate to achieve correct localization of Pex15 to peroxisomes.

Shunsuke Matsumoto, Yoshiki Kogure, Suzuka Ono, Tomoyuki Numata, Toshiya Endo

Abstract read
In one paragraph

Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Overexpression ofInternational journal of molecular sciences · 2026
    Article
  2. Review
  3. 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

5 authors.

Shunsuke MatsumotoDepartment of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.ORCID https://orcid.org/0000-0003-0741-6319
Yoshiki KogureDepartment of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Suzuka OnoFaculty of Life Sciences, Kyoto Sangyo University, Japan.
Tomoyuki NumataDepartment of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.
Toshiya EndoFaculty of Life Sciences, Kyoto Sangyo University, Japan.ORCID https://orcid.org/0000-0001-8548-1584

Funding

Foundation of Kinoshita Memorial EnterpriseJapan Agency for Medical Research and Development 21gm1410002Japan Foundation for Applied EnzymologyJapan Society for the Promotion of Science 15H05705Japan Society for the Promotion of Science 20H00458Japan Society for the Promotion of Science 20H04912Japan Society for the Promotion of Science 20H05689Japan Society for the Promotion of Science 20H05929Japan Society for the Promotion of Science 23H02437Japan Society for the Promotion of Science 23K17995Japan Society for the Promotion of Science 24K18117Japan Society for the Promotion of Science 24KJ0210Takeda Science Foundation
6 · The paper itself

Abstract

Yeast Msp1 is a dual-localized AAA-ATPase on the mitochondrial outer membrane (OM) and peroxisomal membrane. We previously showed that Msp1 transfers mistargeted tail-anchored (TA) proteins from mitochondria to the endoplasmic reticulum (ER) for degradation or delivery to their original destinations. However, the mechanism by which Msp1 in mitochondria and peroxisomes handles authentic peroxisomal TA proteins remains unclear. We show that newly synthesized Pex15 is targeted to peroxisomes primarily via the Pex19- and Pex3-dependent pathway. Mistargeted Pex15 on the mitochondrial OM is extracted by mitochondrial Msp1 and transferred to the ER via the guided-entry of TA proteins pathway for degradation or to peroxisomes via the Pex19-Pex3 pathway. Intriguingly, endogenous Pex15 localized in peroxisomes is also extracted from the membranes by peroxisomal Msp1 but returns to peroxisomes via the Pex19-Pex3 pathway. These results suggest that correct Pex15 localization to peroxisomes relies on not only the initial targeting by Pex19-Pex3 but also the constant re-routing by Msp1 and Pex19-Pex3.

Indexed as

Membrane ProteinsMitochondrial ProteinsPeroxisomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesEndoplasmic ReticulumMitochondriaMitochondrial MembranesPeroxinsPhosphoproteinsProtein TransportAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesMembrane ProteinsMitochondrial ProteinsMSP1 protein, S cerevisiaePeroxinsPEX15 protein, S cerevisiaePEX19 protein, S cerevisiaePEX3 protein, S cerevisiaePhosphoproteinsSaccharomyces cerevisiae ProteinsmitochondriaMsp1peroxisomePex15Pex19‐Pex3

Identifiers

PMID40344504
PMCPMC12366275

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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.