ArticleThe Plant cell2011
The Arabidopsis tail-anchored protein PEROXISOMAL AND MITOCHONDRIAL DIVISION FACTOR1 is involved in the morphogenesis and proliferation of peroxisomes and mitochondria.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 61 citations in OpenAlex.
- Plant organelle division orchestrated by the mosaic machinery of endosymbiotic relics and eukaryotic host factors.Plant physiology · 2026Review
- Comparative observation of mitochondrial morphology in Arabidopsis mutants of 4 reported fission factors.Plant physiology · 2026Article
- Ubiquitin-dependent mitochondrial protein degradation ensures seedling emergence by regulating ER-mitochondrial interaction and mitophagy.Nature plants · 2026Article
- A genome-wide association analysis identifies a key candidate gene controlling plant growth habit in chickpea.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Article
- Peroxisomal-dependent signalling and dynamics modulate plant stress responses: reactive oxygen and nitrogen species as key molecules.Journal of experimental botany · 2025Review
- Plant-specific mitochondrial fission machinery connects mitochondrial dynamics and mitophagosome formation for piecemeal mitophagy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genome-Wide Analysis of C/S1-bZIP Subfamilies inInternational journal of molecular sciences · 2024Article
- TraB family proteins are components of ER-mitochondrial contact sites and regulate ER-mitochondrial interactions and mitophagy.Nature communications · 2022Article
- Article
- A glossary of plant cell structures: Current insights and future questions.The Plant cell · 2022Review
- Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways.Plant physiology · 2021Review
- Contribution of Massive Mitochondrial Fusion and Subsequent Fission in the Plant Life Cycle to the Integrity of the Mitochondrion and Its Genome.International journal of molecular sciences · 2021Review
- E3 ligase, the Oryza sativa salt-induced RING finger protein 4 (OsSIRP4), negatively regulates salt stress responses via degradation of the OsPEX11-1 protein.Plant molecular biology · 2021Article
- Plant Mitophagy in Comparison to Mammals: What Is Still Missing?International journal of molecular sciences · 2021Review
- Miro2 tethers the ER to mitochondria to promote mitochondrial fusion in tobacco leaf epidermal cells.Communications biology · 2020Article
- Pathogenic Bacteria Target Plant Plasmodesmata to Colonize and Invade Surrounding Tissues.The Plant cell · 2020Article
- Dynamics of Peroxisome Homeostasis and Its Role in Stress Response and Signaling in Plants.Frontiers in plant science · 2019Review
- The peroxisome: an update on mysteries 2.0.Histochemistry and cell biology · 2018Review
- Peroxisome Function, Biogenesis, and Dynamics in Plants.Plant physiology · 2018Review
- Fission and Fusion of Plant Mitochondria, and Genome Maintenance.Plant physiology · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peroxisomes and mitochondria are multifunctional eukaryotic organelles that are not only interconnected metabolically but also share proteins in division. Two evolutionarily conserved division factors, dynamin-related protein (DRP) and its organelle anchor FISSION1 (FIS1), mediate the fission of both peroxisomes and mitochondria. Here, we identified and characterized a plant-specific protein shared by these two types of organelles. The Arabidopsis thaliana PEROXISOMAL and MITOCHONDRIAL DIVISION FACTOR1 (PMD1) is a coiled-coil protein tethered to the membranes of peroxisomes and mitochondria by its C terminus. Null mutants of PMD1 contain enlarged peroxisomes and elongated mitochondria, and plants overexpressing PMD1 have an increased number of these organelles that are smaller in size and often aggregated. PMD1 lacks physical interaction with the known division proteins DRP3 and FIS1; it is also not required for DRP3's organelle targeting. Affinity purifications pulled down PMD1's homolog, PMD2, which exclusively targets to mitochondria and plays a specific role in mitochondrial morphogenesis. PMD1 and PMD2 can form homo- and heterocomplexes. Organelle targeting signals reside in the C termini of these proteins. Our results suggest that PMD1 facilitates peroxisomal and mitochondrial proliferation in a FIS1/DRP3-independent manner and that the homologous proteins PMD1 and PMD2 perform nonredundant functions in organelle morphogenesis.
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