ArticleThe FEBS journal2020
Hansenula polymorpha Pex37 is a peroxisomal membrane protein required for organelle fission and segregation.
Article in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024Review
- Convergent and divergent mechanisms of peroxisomal and mitochondrial division.The Journal of cell biology · 2023Article
- Evaluation ofMicroorganisms · 2021Article
- CRISPR-based transcriptional activation tool for silent genes in filamentous fungi.Scientific reports · 2021Article
- Comparative Genomics of Peroxisome Biogenesis Proteins: Making Sense of the PEX Proteins.Frontiers in cell and developmental biology · 2021Article
- Peroxisomal Membrane Contact Sites in Yeasts.Frontiers in cell and developmental biology · 2021Review
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Authors and funding
7 authors at 2 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Here, we describe a novel peroxin, Pex37, in the yeast Hansenula polymorpha. H. polymorpha Pex37 is a peroxisomal membrane protein, which belongs to a protein family that includes, among others, the Neurospora crassa Woronin body protein Wsc, the human peroxisomal membrane protein PXMP2, the Saccharomyces cerevisiae mitochondrial inner membrane protein Sym1, and its mammalian homologue MPV17. We show that deletion of H. polymorpha PEX37 does not appear to have a significant effect on peroxisome biogenesis or proliferation in cells grown at peroxisome-inducing growth conditions (methanol). However, the absence of Pex37 results in a reduction in peroxisome numbers and a defect in peroxisome segregation in cells grown at peroxisome-repressing conditions (glucose). Conversely, overproduction of Pex37 in glucose-grown cells results in an increase in peroxisome numbers in conjunction with a decrease in their size. The increase in numbers in PEX37-overexpressing cells depends on the dynamin-related protein Dnm1. Together our data suggest that Pex37 is involved in peroxisome fission in glucose-grown cells. Introduction of human PXMP2 in H. polymorpha pex37 cells partially restored the peroxisomal phenotype, indicating that PXMP2 represents a functional homologue of Pex37. H.polymorpha pex37 cells did not show aberrant growth on any of the tested carbon and nitrogen sources that are metabolized by peroxisomal enzymes, suggesting that Pex37 may not fulfill an essential function in transport of these substrates or compounds required for their metabolism across the peroxisomal membrane.
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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.