Dynamin-like protein 1 is involved in peroxisomal fission
Open accessAbstract
The mammalian dynamin-like protein 1 (DLP1), a member of the dynamin family of large GTPases, possesses mechanochemical properties known to constrict and tubulate membranes. In this study, we have combined two experimental approaches, induction of peroxisome proliferation by Pex11pbeta and expression of dominant-negative mutants, to test whether DLP1 plays a role in peroxisomal growth and division. We were able to localize DLP1 in spots on tubular peroxisomes in HepG2 cells. In addition, immunoblot analysis revealed the presence of DLP1 in highly purified peroxisomal fractions from rat liver and an increase of DLP1 after treatment of rats with the peroxisome proliferator bezafibrate. Expression of a dominant negative DLP1 mutant deficient in GTP hydrolysis (K38A) either alone or in combination with Pex11pbeta caused the appearance of tubular peroxisomes but had no influence on their intracellular distribution. In co-expressing cells, the formation of tubulo-reticular networks of peroxisomes was promoted, and peroxisomal division was completely inhibited. These findings were confirmed by silencing of DLP1 using siRNA. We propose a direct role for the dynamin-like protein DLP1 in peroxisomal fission and in the maintenance of peroxisomal morphology in mammalian cells.
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Propagation of existing peroxisomes can proceed through self-replication, initiated with PEX11β-dependent elongation of peroxisomal membranes and followed by fission mediated by PEX11β activation of DLP-1.
“Propagation of existing peroxisomes can also proceed through self-replication, initiated with PEX11β-dependent elongation of peroxisomal membranes, and followed by fission mediated by PEX11β activation of the GTPase dynamin-like protein 1, DLP-1 (Koch et al., 2003).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Koch et al., 2003
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Self-citation
- Authors
- Koch, A., Thiemann, M., Grabenbauer, M., Yoon, Y., McNiven, M. A., & Schrader, M.
- Affiliations
- Philipps University of Marburg (DE)
- Heidelberg University (DE)
- Max Planck Society (DE)
- Mayo Clinic (US)
- Corresponding author
- Schrader, Michael
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-03
- Volume
- 278
- Issue
- 10
- Pages
- 8597-8605
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2065060753
- Cited by
- 374
- References
- 61
- Citations by year
- 2026: 6 · 2025: 14 · 2024: 17 · 2023: 24 · 2022: 14 · 2021: 13 · 2020: 20 · 2019: 9 · 2018: 20 · 2017: 17 · 2016: 15 · 2015: 12 · 2014: 17 · 2013: 18 · 2012: 13
- FWCI
- 7.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Johns Hopkins University
- Philipps-Universität Marburg
- Universität Heidelberg
- 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 › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- peroxisome division, peroxisome proliferation, dominant-negative mutant, GTPase, bezafibrate, siRNA knockdown, HepG2 cells, rat liver
- MeSH terms
- Animals, Cell Line, Humans, Microscopy, Fluorescence, Microtubule-Associated Proteins, Proteins, Microscopy, Confocal, GTP Phosphohydrolases, Peroxisomes, Gene Silencing, Mitochondrial Proteins, Dynamins, RNA, Small Interfering, Rats
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