ArticlePlant physiology2025
BTB/POZ-MATH proteins regulate Arabidopsis seedling development by promoting auxin-independent degradation of the Aux/IAA protein IAA10.
Article in Plant physiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- The BTB/POZ-MATH Protein ZmBPM1 Interacts With Autophagy-related Protein ZmATG6 and Modulates the NLR Protein Rp1-D21-Mediated Defense Response in Maize.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The Auxin-Induced Protein Gene (MsARG4) Regulates Rapid Stem Elongation and Nutritional Quality Enhancement in Alfalfa.Plants (Basel, Switzerland) · 2026Article
- Mutational analyses of an instability domain reveal its conserved role in the regulation of class-B ARF levels inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Plant BTB (Broad-Complex, Tramtrack, and Bric-à-Brac) Proteins: Structural Features, Biological Functions, and Roles in Stress Responses.Plants (Basel, Switzerland) · 2026Review
- Ethylene reshapes protein assemblies in the dark.Plant physiology · 2025Article
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Abstract
After germination, seedlings undergo etiolated development (skotomorphogenesis), enabling them to grow toward the soil surface. In Arabidopsis (Arabidopsis thaliana), etiolated seedlings exhibit rapid hypocotyl elongation, apical hook formation, and closed cotyledons to protect the meristem. In this study, we found that high-order mutants in the BPM (BTB/POZ-MATH) gene family displayed defects in seedling development, characterized by a shorter hypocotyl, early apical hook opening, and opened cotyledons in the dark. BPM1, BPM2, BPM4, and BPM5 exhibited distinct expression patterns and subcellular localization in etiolated seedlings. In a hypocotyl segment assay, the bpm mutants showed defects in auxin response, indicating impaired auxin signaling in the hypocotyl. Expression of the auxin reporter DR5:GFP was also altered in the bpm1,4,5 mutant in various tissues compared with the wild type. Furthermore, yeast 2-hybrid, bimolecular fluorescence complementation, and co-immunoprecipitation assay analyses showed that BPM1 interacts with IAA10. Experiments in protoplasts indicated that BPM1 promotes IAA10 ubiquitylation and degradation, which was supported by greater IAA10 protein accumulation in the bpm1,4,5 mutant background. In addition, IAA10 overexpression resulted in phenotypes similar to those of the bpm mutants, indicating that the BPMs may target the Aux/IAA proteins for ubiquitylation and degradation. Overall, our findings shed light on the key roles of the BPMs in auxin signaling during seedling development.
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