Self-Interaction of Human Pex11pβ during Peroxisomal Growth and Division
Open accessAbstract
Pex11 proteins are involved in membrane elongation and division processes associated with the multiplication of peroxisomes. Human Pex11pβ has recently been linked to a new disorder affecting peroxisome morphology and dynamics. Here, we have analyzed the exact membrane topology of Pex11pβ. Studies with an epitope-specific antibody and protease protection assays show that Pex11pβ is an integral membrane protein with two transmembrane domains flanking an internal region exposed to the peroxisomal matrix and N- and C-termini facing the cytosol. A glycine-rich internal region within Pex11pβ is dispensable for peroxisome membrane elongation and division. However, we demonstrate that an amphipathic helix (Helix 2) within the first N-terminal 40 amino acids is crucial for membrane elongation and self-interaction of Pex11pβ. Interestingly, we find that Pex11pβ self-interaction strongly depends on the detergent used for solubilization. We also show that N-terminal cysteines are not essential for membrane elongation, and that putative N-terminal phosphorylation sites are dispensable for Pex11pβ function. We propose that self-interaction of Pex11pβ regulates its membrane deforming activity in conjunction with membrane lipids.
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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 Bonekamp et al., 2013
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References 53 · Cited by 29
- Authors
- Bonekamp, N. A., Grille, S., Cardoso, M. J., Almeida, M., Aroso, M., Gomes, S., Magalhaes, A. C., Ribeiro, D., Islinger, M., & Schrader, M.
- Affiliations
- University of Aveiro (PT)
- University of Exeter (GB)
- Corresponding author
- Schrader, Michael
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-01-07
- Volume
- 8
- Issue
- 1
- Pages
- e53424
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3538539
- OpenAlex
- W1967200055
- Cited by
- 29
- References
- 53
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 3 · 2022: 3 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 1 · 2015: 9 · 2014: 2 · 2013: 1
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Figshare (submittedVersion)
- Open Research Exeter (University of Exeter) (submittedVersion, other-oa)
- Funders
- Deutscher Akademischer Austauschdienst
- Fundação para a Ciência e a Tecnologia (PTDC/BIA-BCM/099613/2008, SFRH/BD/45427/2008, SFRH/BD/80542/2011, SFRH/BD/81223/2011, SFRH/BPD/74428/2010)
- 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 › Lipid Membrane Structure and Behavior
- Keywords
- peroxisome division, protein self-interaction, amphipathic helix, membrane topology, integral membrane proteins, N-terminal cysteine, phosphorylation sites, detergent solubilization, peroxisome biogenesis disorders, membrane deformation
- MeSH terms
- Animals, Chlorocebus aethiops, Humans, Intracellular Membranes, Membrane Proteins, Phosphorylation, Recombinant Fusion Proteins, Transfection, Protein Structure, Secondary, COS Cells, Peroxisomes, Protein Interaction Domains and Motifs
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