ArticleJournal of cell science2023
The dynamin-related protein Vps1 and the peroxisomal membrane protein Pex27 function together during peroxisome fission.
Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Vps1 drives membrane constriction and fission necessary for endosomal protein sorting.The EMBO journal · 2026Article
- Mitochondrial-derived vesicles drive budding-type fission of damaged lysosomes.Nature cell biology · 2026Article
- The trypanosomatid dynamin-like protein associates with glycosomes.bioRxiv : the preprint server for biology · 2026Article
- The yeast peroxisomal proteome at absolute quantitative scale.Histochemistry and cell biology · 2026Article
- Spatiotemporal regulation of organelle transport by spindle position checkpoint kinase Kin4.Journal of cell science · 2024Article
- Convergent and divergent mechanisms of peroxisomal and mitochondrial division.The Journal of cell biology · 2023Article
- Peroxisomal NAD(H) Homeostasis in the YeastBiomolecules · 2023Article
- Spindle Position Checkpoint Kinase Kin4 Regulates Organelle Transport inBiomolecules · 2023Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamin-related proteins (Drps) mediate a variety of membrane remodelling processes. The Saccharomyces cerevisiae Drp, Vps1, is required for endocytosis, endosomal sorting, vacuole fusion, and peroxisome fission and breakdown. How Drps, and in particular Vps1, can function at so many different subcellular locations is of interest to our understanding of cellular organisation. We found that the peroxisomal membrane protein Pex27 is specifically required for Vps1-dependent peroxisome fission in proliferating cells but is not required for Dnm1-dependent peroxisome fission. Pex27 accumulates in constricted regions of peroxisomes and affects peroxisome geometry upon overexpression. Moreover, Pex27 physically interacts with Vps1 in vivo and is required for the accumulation of a GTPase-defective Vps1 mutant (K42A) on peroxisomes. During nitrogen starvation, a condition that halts cell division and induces peroxisome breakdown, Vps1 associates with the pexophagophore. Pex27 is neither required for Vps1 recruitment to the pexophagophore nor for pexophagy. Our study identifies Pex27 as a Vps1-specific partner for the maintenance of peroxisome number in proliferating yeast cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.