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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Peroxisomes have a shared mitochondrial and endoplasmic reticulum origin.
“Peroxisomes have recently been shown to have a shared mitochondrial and endoplasmic reticulum (ER) origin, further linking the function of mitochondria and peroxisomes (Sugiura et al., 2017).”
From NAD+ in Brain Aging and Neurodegenerative Disorders (2019) · cites this paper as Sugiura et al., 2017
In de novo peroxisome synthesis, pre-peroxisomal vesicles bearing PEX16 and PEX3 bud from the endoplasmic reticulum and mitochondria, respectively, and heterotypic fusion establishes pre-peroxisomes competent to import other peroxisomal membrane proteins.
“In de novo synthesis, mature peroxisomes are built incrementally, with the first step a budding of pre-peroxisomal vesicles bearing complementary proteins of the early import machinery, PEX16 and PEX3, from membranes of the endoplasmic reticulum and mitochondria, respectively (Schrader and Pellegrini, 2017; Sugiura et al., 2017). Heterotypic fusion of PEX3- and PEX16-bearing vesicles establish a”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Sugiura et al., 2017
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- 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 · 2016: 1
- 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
- Health Sciences › Medicine › Epidemiology › 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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