ArticleProceedings of the National Academy of Sciences of the United States of America2026
PMF proteins mediate mitochondrial fusion in Arabidopsis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Best practices for biotin ligase-based proximity labeling proteomics in plant systems.The Plant cell · 2026Review
- PERSPECTIVE: organelle positioning as a principle of metabolic regulation and stress tolerance.The Plant journal : for cell and molecular biology · 2026Review
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Authors and funding
7 authors.
Funding
Abstract
Mitochondrial dynamics-continuous fission and fusion-are hallmarks of these organelles and essential for mitochondrial function across eukaryotes. While fission is relatively well understood in plants, the mechanism of fusion remains incompletely defined. In animals and fungi, dynamin-related proteins are emerging fusion factors, but their plant homologs do not localize to mitochondria, suggesting plants rely on a distinct fusion mechanism. Here, we identify PMF1 (Promoter of Mitochondrial Fusion 1) and its paralog PMF2 as plant-specific outer mitochondrial membrane proteins that promote mitochondrial fusion. PMF abundance directly correlates with fusion capacity: overexpression markedly enlarges mitochondria and increases fusion rates, producing megamitochondria, whereas
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