Expression of PEX11β Mediates Peroxisome Proliferation in the Absence of Extracellular Stimuli
Open accessAbstract
Mammalian cells typically contain hundreds of peroxisomes but can increase peroxisome abundance further in response to extracellular stimuli. We report here the identification and characterization of two novel human peroxisomal membrane proteins, PEX11alpha and PEX11beta. Overexpression of the human PEX11beta gene alone was sufficient to induce peroxisome proliferation, demonstrating that proliferation can occur in the absence of extracellular stimuli and may be mediated by a single gene. Time course studies indicated that PEX11beta induces peroxisome proliferation through a multistep process involving peroxisome elongation and segregation of PEX11beta from other peroxisomal membrane proteins, followed by peroxisome division. Overexpression of PEX11alpha also induced peroxisome proliferation but at a much lower frequency than PEX11beta in our experimental system. The patterns of PEX11alpha and PEX11beta expression were examined in the rat, the animal in which peroxisome proliferation has been examined most extensively. Levels of PEX11beta mRNA were similar in all tissues examined and were unaffected by peroxisome-proliferating agents. Conversely, PEX11alpha mRNA levels varied widely among different tissues, were highest in tissues that are sensitive to peroxisome-proliferating agents, and were induced more than 10-fold in response to the peroxisome proliferators clofibrate and di(2-ethylhexyl) phthalate. Taken together, these data implicate PEX11beta in the constitutive control of peroxisome abundance and suggest that PEX11alpha may regulate peroxisome abundance in response to extracellular stimuli.
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PEX11β mediates peroxisome proliferation in the absence of external stimuli and facilitates peroxisome fission by promoting membrane deformation that depends on its self-dimerization.
“PEX11β was shown to mediate peroxisome proliferation in the absence of external stimuli (Schrader et al., 1998). It facilitates peroxisome fission by promoting membrane deformation that depends on its self-dimerization (Bonekamp et al., 2013).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Schrader et al., 1998
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Pex11pβ-mediated growth and division of mammalian peroxisomes follows a maturation pathway
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Self-citationPEX11 proteins attract Mff and hFis1 to coordinate peroxisomal fission
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A role for Mitochondrial Rho GTPase 1 (MIRO1) in motility and membrane dynamics of peroxisomes
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Self-citationTubulo-Reticular Clusters of Peroxisomes in Living COS-7 Cells
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Self-citationPeroxisome Formation and Maintenance Are Dependent on the Endoplasmic Reticulum
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The membrane remodeling protein Pex11p activates the GTPase Dnm1p during peroxisomal fission
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Self-citationPeroxisome Interactions and Cross-Talk with Other Subcellular Compartments in Animal Cells
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Self-citationPeroxisomal ACBD4 interacts with VAPB and promotes ER-peroxisome associations
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Super-resolution Microscopy Reveals Compartmentalization of Peroxisomal Membrane Proteins
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Targeting of hFis1 to Peroxisomes Is Mediated by Pex19p
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PEX13 Is Mutated in Complementation Group 13 of the Peroxisome-Biogenesis Disorders
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Self-citation
- Authors
- Schrader, M., Reuber, B. E., Morrell, J. C., Jimenez-Sanchez, G., Obie, C., Stroh, T. A., Valle, D., Schroer, T. A., & Gould, S. J.
- Affiliations
- Johns Hopkins University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Gould, Stephen J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-11
- Volume
- 273
- Issue
- 45
- Pages
- 29607-29614
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2071649496
- Cited by
- 266
- References
- 22
- Citations by year
- 2026: 8 · 2025: 7 · 2024: 8 · 2023: 5 · 2022: 8 · 2021: 3 · 2020: 9 · 2019: 6 · 2018: 7 · 2017: 8 · 2016: 5 · 2015: 14 · 2014: 11 · 2013: 10 · 2012: 20
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM044589)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK45787, R01DK045787)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- peroxisome proliferation, peroxisome biogenesis, peroxisomal membrane proteins, peroxisome division, clofibrate, DEHP, tissue-specific gene expression, rats
- MeSH terms
- Peroxins, Amino Acid Sequence, Animals, Cell Line, Fungal Proteins, Humans, Membrane Proteins, Microbodies, Molecular Sequence Data, Gene Expression, Sequence Homology, Amino Acid, DNA Primers, DNA, Complementary, Fluorescent Antibody Technique, Indirect, Rats
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