Arabidopsis E3 ubiquitin ligase PLANT U-BOX13 (PUB13) regulates chitin receptor LYSIN MOTIF RECEPTOR KINASE5 (LYK5) protein abundance

Arabidopsis E3 ubiquitin ligase PLANT U-BOX13 (PUB13) regulates chitin receptor LYSIN MOTIF RECEPTOR KINASE5 (LYK5) protein abundance

© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 214(2017), 4 vom: 14. Juni, Seite 1646-1656
1. Verfasser: Liao, Dehua (VerfasserIn)
Weitere Verfasser: Cao, Yangrong, Sun, Xun, Espinoza, Catherine, Nguyen, Cuong T, Liang, Yan, Stacey, Gary
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2017
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article CHITIN ELICITOR RECEPTOR KINASE1 (AtCERK1) E3 ligase LYSIN MOTIF RECEPTOR KINASE5 (AtLYK5) PLANT U-BOX13 (AtPUB13) chitin microbe-associated molecular pattern (MAMP)-triggered immunity protein degradation ubiquitination Arabidopsis Proteins mehr... Oligosaccharides Pathogen-Associated Molecular Pattern Molecules Reactive Oxygen Species chitooctaose oligochitosan Chitin 1398-61-4 Chitosan 9012-76-4 PUB13 protein, Arabidopsis EC 2.3.2.27 Ubiquitin-Protein Ligases LYK5 protein, Arabidopsis EC 2.7.- Protein Kinases
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245 1 0 |a Arabidopsis E3 ubiquitin ligase PLANT U-BOX13 (PUB13) regulates chitin receptor LYSIN MOTIF RECEPTOR KINASE5 (LYK5) protein abundance 
264 1 |c 2017 
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500 |a Date Revised 13.12.2023 
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500 |a Citation Status MEDLINE 
520 |a © 2017 The Authors. New Phytologist © 2017 New Phytologist Trust. 
520 |a Long-chain chitooligosaccharides are fungal microbe-associated molecular patterns (MAMPs) that are recognized by LYSIN MOTIF RECEPTOR KINASE5 (LYK5), inducing the formation of a complex with CHITIN ELICITOR RECEPTOR KINASE1 (CERK1). Formation of this complex leads to activation of the CERK1 intracellular kinase domain and induction of plant innate immunity in Arabidopsis. We found that addition of chitooctaose induced LYK5 protein accumulation as a result of de novo gene expression and the inhibition of LYK5 protein degradation. Screening the putative E3 ligases for interaction with LYK5 identified PLANT U-BOX13 (PUB13), which complexed with LYK5, but this complex dissociated upon addition of chitooctaose. Consistent with these results, LYK5 protein abundance was higher in pub13 mutants compared with the wild type without chitooctaose treatment, while similar abundance was detected with the addition of chitooctaose. The pub13 mutants showed hypersensitivity to chitooctaose-induced rapid responses, such as the production of reactive oxygen species (ROS) and mitogen-activated protein (MAP) kinase phosphorylation, but exhibited normal responses to subsequent long-term chitooctaose treatment, such as gene expression and callose deposition. In addition, PUB13 could ubiquitinate the LYK5 kinase domain in vitro. Taken together, our results suggest an important regulatory function for the turnover of LYK5 mediated by the E3 ligase PUB13 
650 4 |a Journal Article 
650 4 |a CHITIN ELICITOR RECEPTOR KINASE1 (AtCERK1) 
650 4 |a E3 ligase 
650 4 |a LYSIN MOTIF RECEPTOR KINASE5 (AtLYK5) 
650 4 |a PLANT U-BOX13 (AtPUB13) 
650 4 |a chitin 
650 4 |a microbe-associated molecular pattern (MAMP)-triggered immunity 
650 4 |a protein degradation 
650 4 |a ubiquitination 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a Oligosaccharides  |2 NLM 
650 7 |a Pathogen-Associated Molecular Pattern Molecules  |2 NLM 
650 7 |a Reactive Oxygen Species  |2 NLM 
650 7 |a chitooctaose  |2 NLM 
650 7 |a oligochitosan  |2 NLM 
650 7 |a Chitin  |2 NLM 
650 7 |a 1398-61-4  |2 NLM 
650 7 |a Chitosan  |2 NLM 
650 7 |a 9012-76-4  |2 NLM 
650 7 |a PUB13 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.3.2.27  |2 NLM 
650 7 |a Ubiquitin-Protein Ligases  |2 NLM 
650 7 |a EC 2.3.2.27  |2 NLM 
650 7 |a LYK5 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.7.-  |2 NLM 
650 7 |a Protein Kinases  |2 NLM 
650 7 |a EC 2.7.-  |2 NLM 
700 1 |a Cao, Yangrong  |e verfasserin  |4 aut 
700 1 |a Sun, Xun  |e verfasserin  |4 aut 
700 1 |a Espinoza, Catherine  |e verfasserin  |4 aut 
700 1 |a Nguyen, Cuong T  |e verfasserin  |4 aut 
700 1 |a Liang, Yan  |e verfasserin  |4 aut 
700 1 |a Stacey, Gary  |e verfasserin  |4 aut 
773 0 8 |i Enthalten in  |t The New phytologist  |d 1979  |g 214(2017), 4 vom: 14. Juni, Seite 1646-1656  |w (DE-627)NLM09818248X  |x 1469-8137  |7 nnns 
773 1 8 |g volume:214  |g year:2017  |g number:4  |g day:14  |g month:06  |g pages:1646-1656 
856 4 0 |u http://dx.doi.org/10.1111/nph.14472  |3 Volltext 
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