PEX11 family members are membrane elongation factors that coordinate peroxisome proliferation and maintenance
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Dynamic changes of membrane structure are intrinsic to organelle morphogenesis and homeostasis. Ectopic expression of proteins of the PEX11 family from yeast, plant or human lead to the formation of juxtaposed elongated peroxisomes (JEPs),which is evocative of an evolutionary conserved function of these proteins in membrane tubulation. Microscopic examinations reveal that JEPs are composed of independent elongated peroxisomes with heterogeneous distribution of matrix proteins. We established the homo- and heterodimerization properties of the human PEX11 proteins and their interaction with the fission factor hFis1, which is known to recruit the GTPase DRP1 to the peroxisomal membrane. We show that excess of hFis1 but not of DRP1 is sufficient to fragment JEPs into normal round-shaped organelles, and illustrate the requirement of microtubules for JEP formation. Our results demonstrate that PEX11-induced JEPs represent intermediates in the process of peroxisome membrane proliferation and that hFis1 is the limiting factor for progression. Hence, we propose a model for a conserved role of PEX11 proteins in peroxisome maintenance through peroxisome polarization, membrane elongation and segregation.
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PEX11 family members act as membrane elongation factors during peroxisome proliferation.
“With regard to the Pex11-related mouse models, it should be noted that in contrast to the other peroxins, the PEX11 family members act as membrane elongation factors during peroxisome proliferation [70].”
From Peroxisomes in brain development and function (2016) · cites this paper as [70]
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“With regard to the Pex11-related mouse models, it should be noted that in contrast to the other peroxins, the PEX11 family members act as membrane elongation factors during peroxisome proliferation [70].”
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- Authors
- Koch, J., Pranjic, K., Huber, A., Ellinger, A., Hartig, A., Kragler, F., & Brocard, C.
- Affiliations
- University of Vienna (AT)
- Medical University of Vienna (AT)
- Corresponding author
- Brocard, Cécile
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2010-10-01
- Volume
- 123
- Issue
- 19
- Pages
- 3389-3400
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2001847464
- Cited by
- 163
- References
- 66
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 10 · 2023: 7 · 2022: 14 · 2021: 8 · 2020: 6 · 2019: 10 · 2018: 7 · 2017: 8 · 2016: 11 · 2015: 21 · 2014: 9 · 2013: 11 · 2012: 15
- FWCI
- 4.89
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- Phaidra (Universität Wien) (submittedVersion, cc-by-nc-nd)
- HighWire Press Open Archive (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Universidade de Aveiro
- Austrian Science Fund (P20803, P 19682, P 19753)
- Universität Wien
- 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 › Fungal and yeast genetics research
- Keywords
- peroxisome proliferation, microtubules, protein dimerization, membrane tubulation
- MeSH terms
- Genetic Engineering, Humans, Membrane Proteins, Microtubule-Associated Proteins, Microtubules, Protein Binding, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Nicotiana, GTP Phosphohydrolases, Peroxisomes, Cell Surface Extensions, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, Protein Multimerization, HEK293 Cells
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