ArticleMolecular plant pathology2022
Deubiquitinase Ubp3 regulates ribophagy and deubiquitinates Smo1 for appressorium-mediated infection by Magnaporthe oryzae.
Article in Molecular plant pathology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 16 citations in OpenAlex.
- The interaction between CfAda3 and CfGcn5 impacts growth, development, and virulence ofVirulence · 2026Article
- Histone Demethylase MoRph1 Regulates Fungal Development, Pathogenicity, and DNA Damage Repair inJournal of fungi (Basel, Switzerland) · 2026Article
- Deubiquitinase MoAMSH inhibits autophagy by targeting MoAtg6 in Magnaporthe oryzae.Cell communication and signaling : CCS · 2025Article
- Functional Characterization of Deubiquitinase UBP Family and Proteomic Analysis of Aaubp14-Mediated Pathogenicity Mechanism inJournal of fungi (Basel, Switzerland) · 2025Article
- Appressoria-Small but Incredibly Powerful Structures in Plant-Pathogen Interactions.International journal of molecular sciences · 2023Review
- Review
- Deubiquitinase Ubp3 regulates ribophagy and deubiquitinates Smo1 for appressorium-mediated infection by Magnaporthe oryzae.Molecular plant pathology · 2022Article
- The Deubiquitinating EnzymeFrontiers in fungal biology · 2022Article
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Authors and funding
13 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The Ubp family of deubiquitinating enzymes has been found to play important roles in plant-pathogenic fungi, but their regulatory mechanisms are still largely unknown. In this study, we revealed the regulatory mechanism of the deubiquitinating enzyme Ubp3 during the infection process of Magnaporthe oryzae. AUBP3 deletion mutant was severely defective in appressorium turgor accumulation, leading to the impairment of appressorial penetration. During appressorium formation, the mutant was also defective in glycogen and lipid metabolism. Interestingly, we found that nitrogen starvation and rapamycin treatment induced the ribophagy process in M. oryzae, which is closely dependent on Ubp3. In the ∆ubp3 mutant, the ribosome proteins and rRNAs were not well degraded on nitrogen starvation and rapamycin treatment. We also found that Ubp3 interacted with the GTPase-activating protein Smo1 and regulated its de-ubiquitination. Ubp3-dependent de-ubiquitination of Smo1 may be required for Smo1 to coordinate Ras signalling. Taken together, our results showed at least two roles of Ubp3 in M. oryzae: it regulates the ribophagy process and it regulates de-ubiquitination of GTPase-activating protein Smo1 for appressorium-mediated infection.
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