Cited by 389Cellular transport and secretionAutophagy in Disease and TherapyMitochondrial Function and Pathology

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

Newly born peroxisomes are a hybrid of mitochondrial and ER-derived pre-peroxisomes

Abstract

Peroxisomes function together with mitochondria in a number of essential biochemical pathways, from bile acid synthesis to fatty acid oxidation. Peroxisomes grow and divide from pre-existing organelles, but can also emerge de novo in the cell. The physiological regulation of de novo peroxisome biogenesis remains unclear, and it is thought that peroxisomes emerge from the endoplasmic reticulum in both mammalian and yeast cells. However, in contrast to the yeast system, a number of integral peroxisomal membrane proteins are imported into mitochondria in mammalian cells in the absence of peroxisomes, including Pex3, Pex12, Pex13, Pex14, Pex26, PMP34 and ALDP. Overall, the mitochondrial localization of peroxisomal membrane proteins in mammalian cells has largely been considered a mis-targeting artefact in which de novo biogenesis occurs exclusively from endoplasmic reticulum-targeted peroxins. Here, in following the generation of new peroxisomes within human patient fibroblasts lacking peroxisomes, we show that the essential import receptors Pex3 and Pex14 target mitochondria, where they are selectively released into vesicular pre-peroxisomal structures. Maturation of pre-peroxisomes containing Pex3 and Pex14 requires fusion with endoplasmic reticulum-derived vesicles carrying Pex16, thereby providing full import competence. These findings demonstrate the hybrid nature of newly born peroxisomes, expanding their functional links to mitochondria.

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Crossref · 10.1038/nature21375

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Metadata

Authors
Sugiura, A., Mattie, S., Prudent, J., & McBride, H. M.
Affiliations
Montreal Neurological Institute and Hospital (CA)
Corresponding author
McBride, Heidi M.
Venue
Nature
Published
2017-02-01
Volume
542
Issue
7640
Pages
251-254
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W2585343016
Cited by
386
References
38
Citations by year
2026: 26 · 2025: 25 · 2024: 26 · 2023: 42 · 2022: 47 · 2021: 46 · 2020: 42 · 2019: 44 · 2018: 53 · 2017: 34
FWCI
25.24
Type
journal article
Language
en
Open access
closed
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords
peroxisome biogenesis, PEX3, PEX14, PEX16, PEX12, PEX13, ALDP, peroxisomal membrane proteins, mitochondrial targeting, endoplasmic reticulum
MeSH terms
Peroxins, Bacterial Proteins, Organelle Biogenesis, Cell Line, Endoplasmic Reticulum, Fibroblasts, Humans, Intracellular Membranes, Lipoproteins, Luminescent Proteins, Membrane Proteins, Mitochondria, Repressor Proteins, Zellweger Syndrome, Peroxisomes, Protein Transport

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