Peroxisome degradation in mammals: mechanisms of action, recent advances, and perspectives
Open accessAbstract
Peroxisomes are remarkably dynamic organelles that participate in a diverse array of cellular processes, including the metabolism of lipids and reactive oxygen species. In order to regulate peroxisome function in response to changing nutritional and environmental stimuli, new organelles need to be formed and superfluous and dysfunctional organelles have to be selectively removed. Disturbances in any of these processes have been associated with the etiology and progression of various congenital neurodegenerative and age-related human disorders. The aim of this review is to critically explore our current knowledge of how peroxisomes are degraded in mammalian cells and how defects in this process may contribute to human disease. Some of the key issues highlighted include the current concepts of peroxisome removal, the peroxisome quality control mechanisms, the initial triggers for peroxisome degradation, the factors for dysfunctional peroxisome recognition, and the regulation of peroxisome homeostasis. We also dissect the functional and mechanistic relationship between different forms of selective organelle degradation and consider how lysosomal dysfunction may lead to defects in peroxisome turnover. In addition, we draw lessons from studies on other organisms and extrapolate this knowledge to mammals. Finally, we discuss the potential pathological implications of dysfunctional peroxisome degradation for human health.
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Peroxisomes are degraded by regulated autophagy and to a lesser extent by peroxisomal LONP2-mediated proteolysis and lipoxygenase 15-mediated membrane disruption.
“Peroxisomes are degraded by regulated autophagy (Deosaran et al., 2013; Nordgren et al., 2013) and to a lesser extent, peroxisomal Lon peptidase 2 (LONP2)-mediated proteolysis, and membrane disruption that is mediated by lipoxygenase 15 (Yokota et al., 2001; Yokota and Fahimi, 2009; Walker et al., 2018).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Nordgren et al., 2013
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Antiinflammatory Effects of Hydrogen Peroxide in Neutrophil Activation and Acute Lung Injury
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Functional Domains and Dynamic Assembly of the Peroxin Pex14p, the Entry Site of Matrix Proteins
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Self-citationPeroxisome Proliferators‐Activated Receptor (PPAR) Modulators and Metabolic Disorders
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Pex11pβ-mediated growth and division of mammalian peroxisomes follows a maturation pathway
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Getting a camel through the eye of a needle: the import of folded proteins by peroxisomes
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Peroxisomal Impairment in Niemann-Pick Type C Disease
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Catalase transgenic mice: characterization and sensitivity to oxidative stress
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Receptor Proteins in Selective Autophagy
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Yeast and filamentous fungi as model organisms in microbody research
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Peroxisome Size Provides Insights into the Function of Autophagy-related Proteins
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Autophagic degradation of peroxisomes in isolated rat hepatocytes
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Insulin-Degrading Enzyme Exists Inside of Rat Liver Peroxisomes and Degrades Oxidized Proteins.
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Pex14 is the sole component of the peroxisomal translocon that is required for pexophagy
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Renal cell carcinoma and oxidative stress: The lack of peroxisomes
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Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone
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Docosahexaenoic acid mediates peroxisomal elongation, a prerequisite for peroxisome division
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Peroxisomes, cell senescence, and rates of aging
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Alternative Macroautophagic Pathways
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Integration of peroxisomes into an endomembrane system that governs cellular aging
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Genetic Dissection of Peroxisome-Associated Matrix Protein Degradation in Arabidopsis thaliana
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Hypocatalasemic Fibroblasts Accumulate Hydrogen Peroxide and Display Age-Associated Pathologies
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The exportomer: the peroxisomal receptor export machinery
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Nbr1 Is a Novel Inhibitor of Ligand-Mediated Receptor Tyrosine Kinase Degradation
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Expression of the Hydrogen Peroxide-Generating Enzyme Fatty Acyl CoA Oxidase Activates NF-kappa B
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The music of lipids: How lipid composition orchestrates cellular behaviour
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Cytosolic factors mediate protein insertion into the peroxisomal membrane
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Lumenal peroxisomal protein aggregates are removed by concerted fission and autophagy events
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Peroxisome Morphology in Pathologies
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Damaged peroxisomes are subject to rapid autophagic degradation in the yeastHansenula polymorpha
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Protein Structure and Import Into the Peroxisomal Matrix
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Up for grabs; trashing peroxisomes
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Flagged first, then by citations
Research works printed but not linked: 1
- Rhodin J. (1954). Correlation of Ultrastructural Organization and Function in Normal and Experimentally Changed Proximal Tubule Cells of the Mouse Kidney. Doctorate. Thesis, Karolinska Institutet, Stockholm
Cited by
Sorted by citations
The cell biology of the retinal pigment epithelium
Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422 · see citing works
The Peroxisome-Mitochondria Connection: How and Why?
Fransen, M., Lismont, C., & Walton, P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061126 · Cited by 351 · see citing works
“Damaged or superfluous peroxisomes are mainly degraded by the autophagy-lysosome pathway, in a process known as pexophagy [21,22].”
BackgroundSelf-citationPeroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagy
Nazarko, T. Y., Ozeki, K., Till, A., Ramakrishnan, G., Lotfi, P., Yan, M., & Subramani, S. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201307050 · Cited by 99 · see citing works
- Authors
- Nordgren, M., Wang, B., Apanasets, O., & Fransen, M.
- Affiliations
- KU Leuven (BE)
- Corresponding author
- Fransen, Marc
- Venue
- Frontiers in Physiology
- Publisher
- Frontiers Media SA
- Published
- 2013
- Volume
- 4
- Pages
- 145-145
- ISSN
- 1664-042X (ISSN-L)
- PMC
- PMC3682127
- OpenAlex
- W1993630264
- Cited by
- 67
- References
- 148
- Citations by year
- 2026: 3 · 2025: 2 · 2023: 3 · 2022: 5 · 2021: 6 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 8 · 2016: 7 · 2015: 7 · 2014: 12 · 2013: 4
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Physiology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Lirias (acceptedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- KU Leuven (OT/09/045)
- Vlaamse regering
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- peroxisome degradation, selective autophagy, lysosomal dysfunction, peroxisome biogenesis disorders, neurodegenerative diseases, age-related diseases, reactive oxygen species metabolism, lipid metabolism
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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