ArticleScience advances2024
A dynamic ubiquitination balance of cell proliferation and endoreduplication regulators determines plant organ size.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Ubiquitination-Mediated Regulation of Brassinosteroid Signaling.Plants (Basel, Switzerland) · 2026Review
- Ubiquitination of the ribosomal-like domain of UBIQUITIN6 contributes to cell wall stress responses in Arabidopsis.The Plant cell · 2026Article
- Article
- Aging drives a program of DNA methylation decay in plant organs.Science (New York, N.Y.) · 2026Article
- The Ubiquitin Script: writing protein fates in chains.Essays in biochemistry · 2025Review
- Multifaceted roles of TaGW2 in wheat growth-defense trade-offs.Plant communications · 2025Article
- TaGW2-TaVOZ1 module regulates wheat salt tolerance via both E3 ligase-dependent and -independent pathways.Science advances · 2025Article
- Membrane-associated ring-CH-type finger 2 protects against metabolic dysfunction-associated fatty liver disease by targeting fatty acid synthase.Molecular metabolism · 2025Article
- When Size Matters: New Insights on How Seed Size Can Contribute to the Early Stages of Plant Development.Plants (Basel, Switzerland) · 2024Review
- An insight into the roles of ubiquitin-specific proteases in plants: development and growth, morphogenesis, and stress response.Frontiers in plant science · 2024Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitination plays a crucial role throughout plant growth and development. The E3 ligase DA2 has been reported to activate the peptidase DA1 by ubiquitination, hereby limiting cell proliferation. However, the molecular mechanisms that regulate DA2 remain elusive. Here, we demonstrate that DA2 has a very high turnover and auto-ubiquitinates with K48-linkage polyubiquitin chains, which is counteracted by two deubiquitinating enzymes, UBIQUITIN-SPECIFIC PROTEASE 12 (UBP12) and UBP13. Unexpectedly, we found that auto-ubiquitination of DA2 does not influence its stability but determines its E3 ligase activity. We also demonstrate that impairing the protease activity of DA1 abolishes the growth-reducing effect of DA2. Last, we show that synthetic, constitutively activated DA1-ubiquitin fusion proteins overrule this complex balance of ubiquitination and deubiquitination and strongly restrict growth and promote endoreduplication. Our findings highlight a nonproteolytic function of K48-linked polyubiquitination and reveal a mechanism by which DA2 auto-ubiquitination levels, in concert with UBP12 and UBP13, precisely monitor the activity of DA1 and fine-tune plant organ size.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.