ArticleThe Plant cell2024
Active protein ubiquitination regulates xylem vessel functionality.
Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Multiomics analyses of mutants for Marchantia polymorpha FERONIA and MARIS reveal a link between cell wall integrity and abscisic acid responses.Plant & cell physiology · 2026Article
- Salicylic acid-mediated competitive regulation of xylem vessel formation and defense responses in Arabidopsis thaliana.Plant & cell physiology · 2025Article
- The role of VND transcription factors in xylem vessel development and secondary wall formation.The New phytologist · 2025Review
- LRM3 positively regulates stem lodging resistance by degradating MYB6 transcriptional repressor in soybean.Plant biotechnology journal · 2025Article
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9 authors.
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Abstract
Xylem vessels function in the long-distance conduction of water in land plants. The NAC transcription factor VASCULAR-RELATED NAC-DOMAIN7 (VND7) is a master regulator of xylem vessel cell differentiation in Arabidopsis (Arabidopsis thaliana). We previously isolated suppressor of ectopic xylem vessel cell differentiation induced by VND7 (seiv) mutants. Here, we report that the responsible genes for seiv3, seiv4, seiv6, and seiv9 are protein ubiquitination-related genes encoding PLANT U-BOX46 (PUB46), an uncharacterized F-BOX protein (FBX), PUB36, and UBIQUITIN-SPECIFIC PROTEASE1 (UBP1), respectively. We also found decreased expression of genes downstream of VND7 and abnormal xylem transport activity in the seiv mutants. Upon VND7 induction, ubiquitination levels from 492 and 180 protein groups were upregulated and downregulated, respectively. VND7 induction resulted in the ubiquitination of proteins for cell wall biosynthesis and protein transport, whereas such active protein ubiquitination did not occur in the seiv mutants. We detected the ubiquitination of three lysine residues in VND7: K94, K105, and K260. Substituting K94 with arginine significantly decreased the transactivation activity of VND7, suggesting that the ubiquitination of K94 is crucial for regulating VND7 activity. Our findings highlight the crucial roles of target protein ubiquitination in regulating xylem vessel activity.
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