ArticleProceedings of the National Academy of Sciences of the United States of America2026
Ubiquitination of BAM1 attenuates CLE peptide-mediated signaling in the root apical meristem.
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 1 paper.
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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
1 citing paper in PubMed.
- The ubiquitin code of receptor kinases in plants.Journal of integrative plant biology · 2026Review
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Authors and funding
9 authors.
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Abstract
The plasma membrane-resident receptor-like kinases (RLKs) and their cognate peptide ligands play crucial roles in plant growth and development. The RLK BARELY ANY MERISTEM1 (BAM1) promotes phloem formation and regulates other aspects of root development. However, the mechanisms governing BAM1 protein degradation remain unclear. In this study, we demonstrate that two closely related ubiquitin ligases, RING DOMAIN LIGASE 1 (RGLG1) and RGLG2, specifically interact with BAM1 and its closest homolog BAM2. RGLG1/2 ubiquitinate BAM1/2 and mediate their degradation, thereby dampening BAM1/2 signaling. Treatment with the peptide CLE13 (CLV3/EMBRYO SURROUNDING REGION-RELATED 13) enhances the BAM1/2-RGLG2 interaction and the ubiquitin ligase activity of RGLG2, resulting in increased ubiquitination and degradation of BAM1/2 by RGLG1/2. The
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