Csn5 inhibits autophagy by regulating the ubiquitination of Atg6 and Tor to mediate the pathogenicity of Magnaporthe oryzae
© 2024. The Author(s)..
Csn5 is subunit 5 of the COP9 signalosome (CSN), but the mechanism by which it strictly controls the pathogenicity of pathogenic fungi through autophagy remains unclear. Here, we found that Csn5 deficiency attenuated pathogenicity and enhanced autophagy in Magnaporthe oryzae. MoCSN5 knockout led to overubiquitination and overdegradation of MoTor (the core protein of the TORC1 complex [target of rapamycin]) thereby promoted autophagy. In addition, we identified MoCsn5 as a new interactor of MoAtg6. Atg6 was found to be ubiquitinated through linkage with lysine 48 (K48) in cells, which is necessary for infection-associated autophagy in pathogenic fungi. K48-ubiquitination of Atg6 enhanced its degradation and thereby inhibited autophagic activity. Our experimental results indicated that MoCsn5 promoted K48-ubiquitination of MoAtg6, which reduced the MoAtg6 protein content and thus inhibited autophagy. Aberrant ubiquitination and autophagy in ΔMocsn5 led to pleiotropic defects in the growth, development, stress resistance, and pathogenicity of M. oryzae. In summary, our study revealed a novel mechanism by which Csn5 regulates autophagy and pathogenicity in rice blast fungus through ubiquitination.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:22 |
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| Enthalten in: |
Cell communication and signaling : CCS - 22(2024), 1 vom: 09. Apr., Seite 222 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Shen, Zi-Fang [VerfasserIn] |
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| Links: |
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| Themen: |
Autophagy |
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| Anmerkungen: |
Date Completed 11.04.2024 Date Revised 12.04.2024 published: Electronic Citation Status MEDLINE |
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| doi: |
10.1186/s12964-024-01598-7 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM370841085 |
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| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2024. The Author(s). | ||
| 520 | |a Csn5 is subunit 5 of the COP9 signalosome (CSN), but the mechanism by which it strictly controls the pathogenicity of pathogenic fungi through autophagy remains unclear. Here, we found that Csn5 deficiency attenuated pathogenicity and enhanced autophagy in Magnaporthe oryzae. MoCSN5 knockout led to overubiquitination and overdegradation of MoTor (the core protein of the TORC1 complex [target of rapamycin]) thereby promoted autophagy. In addition, we identified MoCsn5 as a new interactor of MoAtg6. Atg6 was found to be ubiquitinated through linkage with lysine 48 (K48) in cells, which is necessary for infection-associated autophagy in pathogenic fungi. K48-ubiquitination of Atg6 enhanced its degradation and thereby inhibited autophagic activity. Our experimental results indicated that MoCsn5 promoted K48-ubiquitination of MoAtg6, which reduced the MoAtg6 protein content and thus inhibited autophagy. Aberrant ubiquitination and autophagy in ΔMocsn5 led to pleiotropic defects in the growth, development, stress resistance, and pathogenicity of M. oryzae. In summary, our study revealed a novel mechanism by which Csn5 regulates autophagy and pathogenicity in rice blast fungus through ubiquitination | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Autophagy | |
| 650 | 4 | |a COP9 signalosome | |
| 650 | 4 | |a Csn5 | |
| 650 | 4 | |a Pathogenicity | |
| 650 | 4 | |a Rice blast fungus | |
| 650 | 4 | |a Ubiquitination | |
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| 700 | 1 | |a Li, Lin |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Jing-Yi |e verfasserin |4 aut | |
| 700 | 1 | |a Liao, Jian |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Yun-Ran |e verfasserin |4 aut | |
| 700 | 1 | |a Zhu, Xue-Ming |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Zi-He |e verfasserin |4 aut | |
| 700 | 1 | |a Lu, Jian-Ping |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Xiao-Hong |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Fu-Cheng |e verfasserin |4 aut | |
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