An F‐box protein attenuates fungal xylanase‐triggered immunity by destabilizing LRR‐RLP NbEIX2 in a SOBIR1‐dependent manner
Summary Receptor‐like proteins (RLPs) lacking the cytoplasmic kinase domain play crucial roles in plant growth, development and immunity. However, what remains largely elusive is whether RLP protein levels are fine‐tuned by E3 ubiquitin ligases, which are employed by receptor‐like kinases for signal...
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| Veröffentlicht in: | The New phytologist 2022-12, Vol.236 (6), p.2202-2215 |
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| container_title | The New phytologist |
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| creator | Wang, Nan Yin, Zhiyuan Zhao, Yaning Wang, Jinghao Pei, Yong Ji, Peiyun Daly, Paul Li, Zhengpeng Dou, Daolong Wei, Lihui |
| description | Summary
Receptor‐like proteins (RLPs) lacking the cytoplasmic kinase domain play crucial roles in plant growth, development and immunity. However, what remains largely elusive is whether RLP protein levels are fine‐tuned by E3 ubiquitin ligases, which are employed by receptor‐like kinases for signaling attenuation. Nicotiana benthamiana NbEIX2 is a leucine‐rich repeat RLP (LRR‐RLP) that mediates fungal xylanase‐triggered immunity.
Here we show that NbEIX2 associates with an F‐box protein NbPFB1, which promotes NbEIX2 degradation likely by forming an SCF E3 ubiquitin ligase complex, and negatively regulates NbEIX2‐mediated immune responses.
NbEIX2 undergoes ubiquitination and proteasomal degradation in planta. Interestingly, NbEIX2 without its cytoplasmic tail is still associated with and destabilized by NbPFB1. In addition, NbPFB1 also associates with and destabilizes NbSOBIR1, a co‐receptor of LRR‐RLPs, and fails to promote NbEIX2 degradation in the sobir1 mutant.
Our findings reveal a distinct model of NbEIX2 degradation, in which an F‐box protein destabilizes NbEIX2 indirectly in a SOBIR1‐dependent manner. |
| doi_str_mv | 10.1111/nph.18509 |
| format | Article |
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Receptor‐like proteins (RLPs) lacking the cytoplasmic kinase domain play crucial roles in plant growth, development and immunity. However, what remains largely elusive is whether RLP protein levels are fine‐tuned by E3 ubiquitin ligases, which are employed by receptor‐like kinases for signaling attenuation. Nicotiana benthamiana NbEIX2 is a leucine‐rich repeat RLP (LRR‐RLP) that mediates fungal xylanase‐triggered immunity.
Here we show that NbEIX2 associates with an F‐box protein NbPFB1, which promotes NbEIX2 degradation likely by forming an SCF E3 ubiquitin ligase complex, and negatively regulates NbEIX2‐mediated immune responses.
NbEIX2 undergoes ubiquitination and proteasomal degradation in planta. Interestingly, NbEIX2 without its cytoplasmic tail is still associated with and destabilized by NbPFB1. In addition, NbPFB1 also associates with and destabilizes NbSOBIR1, a co‐receptor of LRR‐RLPs, and fails to promote NbEIX2 degradation in the sobir1 mutant.
Our findings reveal a distinct model of NbEIX2 degradation, in which an F‐box protein destabilizes NbEIX2 indirectly in a SOBIR1‐dependent manner.</description><identifier>ISSN: 0028-646X</identifier><identifier>EISSN: 1469-8137</identifier><identifier>DOI: 10.1111/nph.18509</identifier><identifier>PMID: 36151918</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Degradation ; E3 ligase ; F-Box Proteins ; Fungi ; Immune response ; Immunity ; Kinases ; Leucine ; Nicotiana - genetics ; Nicotiana - microbiology ; Nicotiana benthamiana ; pattern‐triggered immunity ; Phosphotransferases ; Plant growth ; Proteasomes ; Protein Domains ; Proteins ; Receptors ; SCF complex ; Signal Transduction ; Ubiquitin ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligases ; Ubiquitination ; Xylanase</subject><ispartof>The New phytologist, 2022-12, Vol.236 (6), p.2202-2215</ispartof><rights>2022 The Authors. © 2022 New Phytologist Foundation.</rights><rights>2022 The Authors. New Phytologist © 2022 New Phytologist Foundation.</rights><rights>Copyright © 2022 New Phytologist Trust</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3539-d01b99f5f51091091859d2ed4e69c592b1448997692221d5d59160eda1136a893</citedby><cites>FETCH-LOGICAL-c3539-d01b99f5f51091091859d2ed4e69c592b1448997692221d5d59160eda1136a893</cites><orcidid>0000-0001-5226-6642 ; 0000-0002-7189-895X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fnph.18509$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fnph.18509$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36151918$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Nan</creatorcontrib><creatorcontrib>Yin, Zhiyuan</creatorcontrib><creatorcontrib>Zhao, Yaning</creatorcontrib><creatorcontrib>Wang, Jinghao</creatorcontrib><creatorcontrib>Pei, Yong</creatorcontrib><creatorcontrib>Ji, Peiyun</creatorcontrib><creatorcontrib>Daly, Paul</creatorcontrib><creatorcontrib>Li, Zhengpeng</creatorcontrib><creatorcontrib>Dou, Daolong</creatorcontrib><creatorcontrib>Wei, Lihui</creatorcontrib><title>An F‐box protein attenuates fungal xylanase‐triggered immunity by destabilizing LRR‐RLP NbEIX2 in a SOBIR1‐dependent manner</title><title>The New phytologist</title><addtitle>New Phytol</addtitle><description>Summary
Receptor‐like proteins (RLPs) lacking the cytoplasmic kinase domain play crucial roles in plant growth, development and immunity. However, what remains largely elusive is whether RLP protein levels are fine‐tuned by E3 ubiquitin ligases, which are employed by receptor‐like kinases for signaling attenuation. Nicotiana benthamiana NbEIX2 is a leucine‐rich repeat RLP (LRR‐RLP) that mediates fungal xylanase‐triggered immunity.
Here we show that NbEIX2 associates with an F‐box protein NbPFB1, which promotes NbEIX2 degradation likely by forming an SCF E3 ubiquitin ligase complex, and negatively regulates NbEIX2‐mediated immune responses.
NbEIX2 undergoes ubiquitination and proteasomal degradation in planta. Interestingly, NbEIX2 without its cytoplasmic tail is still associated with and destabilized by NbPFB1. In addition, NbPFB1 also associates with and destabilizes NbSOBIR1, a co‐receptor of LRR‐RLPs, and fails to promote NbEIX2 degradation in the sobir1 mutant.
Our findings reveal a distinct model of NbEIX2 degradation, in which an F‐box protein destabilizes NbEIX2 indirectly in a SOBIR1‐dependent manner.</description><subject>Degradation</subject><subject>E3 ligase</subject><subject>F-Box Proteins</subject><subject>Fungi</subject><subject>Immune response</subject><subject>Immunity</subject><subject>Kinases</subject><subject>Leucine</subject><subject>Nicotiana - genetics</subject><subject>Nicotiana - microbiology</subject><subject>Nicotiana benthamiana</subject><subject>pattern‐triggered immunity</subject><subject>Phosphotransferases</subject><subject>Plant growth</subject><subject>Proteasomes</subject><subject>Protein Domains</subject><subject>Proteins</subject><subject>Receptors</subject><subject>SCF complex</subject><subject>Signal Transduction</subject><subject>Ubiquitin</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitin-Protein Ligases</subject><subject>Ubiquitination</subject><subject>Xylanase</subject><issn>0028-646X</issn><issn>1469-8137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp10cFqFDEYB_Agil2rB19AAl70MG2-ZJKZHGtp7cLSllWhtyGz-WZNmclskxnseBL6An1Gn8Ss23ooGAI55MeffPkT8hbYAaR16DffD6CUTD8jM8iVzkoQxXMyY4yXmcrV1R55FeM1Y0xLxV-SPaFAgoZyRu6OPD39_eu-7m_pJvQDOk_NMKAfzYCRNqNfm5beTq3xJmKCQ3DrNQa01HXd6N0w0XqiFuNgate6n86v6WK5THK5uKTn9cn8itNtKP1y8Wm-hHRhcYPeoh9oZ7zH8Jq8aEwb8c3DuU--nZ58PT7LFhef58dHi2wlpNCZZVBr3chGAtPbXUptOdoclV5JzWvI81LrQmnOOVhppQbF0BoAoUypxT75sMtNg96M6cVV5-IK2zQb9mOseAGFKgUUW_r-Cb3ux-DT65ISRfpYJURSH3dqFfoYAzbVJrjOhKkCVm2bqVIz1d9mkn33kDjWHdp_8rGKBA534Idrcfp_UnV-ebaL_AMHlJnp</recordid><startdate>202212</startdate><enddate>202212</enddate><creator>Wang, Nan</creator><creator>Yin, Zhiyuan</creator><creator>Zhao, Yaning</creator><creator>Wang, Jinghao</creator><creator>Pei, Yong</creator><creator>Ji, Peiyun</creator><creator>Daly, Paul</creator><creator>Li, Zhengpeng</creator><creator>Dou, Daolong</creator><creator>Wei, Lihui</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7SN</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-5226-6642</orcidid><orcidid>https://orcid.org/0000-0002-7189-895X</orcidid></search><sort><creationdate>202212</creationdate><title>An F‐box protein attenuates fungal xylanase‐triggered immunity by destabilizing LRR‐RLP NbEIX2 in a SOBIR1‐dependent manner</title><author>Wang, Nan ; Yin, Zhiyuan ; Zhao, Yaning ; Wang, Jinghao ; Pei, Yong ; Ji, Peiyun ; Daly, Paul ; Li, Zhengpeng ; Dou, Daolong ; Wei, Lihui</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3539-d01b99f5f51091091859d2ed4e69c592b1448997692221d5d59160eda1136a893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Degradation</topic><topic>E3 ligase</topic><topic>F-Box Proteins</topic><topic>Fungi</topic><topic>Immune response</topic><topic>Immunity</topic><topic>Kinases</topic><topic>Leucine</topic><topic>Nicotiana - genetics</topic><topic>Nicotiana - microbiology</topic><topic>Nicotiana benthamiana</topic><topic>pattern‐triggered immunity</topic><topic>Phosphotransferases</topic><topic>Plant growth</topic><topic>Proteasomes</topic><topic>Protein Domains</topic><topic>Proteins</topic><topic>Receptors</topic><topic>SCF complex</topic><topic>Signal Transduction</topic><topic>Ubiquitin</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitin-Protein Ligases</topic><topic>Ubiquitination</topic><topic>Xylanase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Nan</creatorcontrib><creatorcontrib>Yin, Zhiyuan</creatorcontrib><creatorcontrib>Zhao, Yaning</creatorcontrib><creatorcontrib>Wang, Jinghao</creatorcontrib><creatorcontrib>Pei, Yong</creatorcontrib><creatorcontrib>Ji, Peiyun</creatorcontrib><creatorcontrib>Daly, Paul</creatorcontrib><creatorcontrib>Li, Zhengpeng</creatorcontrib><creatorcontrib>Dou, Daolong</creatorcontrib><creatorcontrib>Wei, Lihui</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The New phytologist</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Nan</au><au>Yin, Zhiyuan</au><au>Zhao, Yaning</au><au>Wang, Jinghao</au><au>Pei, Yong</au><au>Ji, Peiyun</au><au>Daly, Paul</au><au>Li, Zhengpeng</au><au>Dou, Daolong</au><au>Wei, Lihui</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An F‐box protein attenuates fungal xylanase‐triggered immunity by destabilizing LRR‐RLP NbEIX2 in a SOBIR1‐dependent manner</atitle><jtitle>The New phytologist</jtitle><addtitle>New Phytol</addtitle><date>2022-12</date><risdate>2022</risdate><volume>236</volume><issue>6</issue><spage>2202</spage><epage>2215</epage><pages>2202-2215</pages><issn>0028-646X</issn><eissn>1469-8137</eissn><abstract>Summary
Receptor‐like proteins (RLPs) lacking the cytoplasmic kinase domain play crucial roles in plant growth, development and immunity. However, what remains largely elusive is whether RLP protein levels are fine‐tuned by E3 ubiquitin ligases, which are employed by receptor‐like kinases for signaling attenuation. Nicotiana benthamiana NbEIX2 is a leucine‐rich repeat RLP (LRR‐RLP) that mediates fungal xylanase‐triggered immunity.
Here we show that NbEIX2 associates with an F‐box protein NbPFB1, which promotes NbEIX2 degradation likely by forming an SCF E3 ubiquitin ligase complex, and negatively regulates NbEIX2‐mediated immune responses.
NbEIX2 undergoes ubiquitination and proteasomal degradation in planta. Interestingly, NbEIX2 without its cytoplasmic tail is still associated with and destabilized by NbPFB1. In addition, NbPFB1 also associates with and destabilizes NbSOBIR1, a co‐receptor of LRR‐RLPs, and fails to promote NbEIX2 degradation in the sobir1 mutant.
Our findings reveal a distinct model of NbEIX2 degradation, in which an F‐box protein destabilizes NbEIX2 indirectly in a SOBIR1‐dependent manner.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>36151918</pmid><doi>10.1111/nph.18509</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0001-5226-6642</orcidid><orcidid>https://orcid.org/0000-0002-7189-895X</orcidid></addata></record> |
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| ispartof | The New phytologist, 2022-12, Vol.236 (6), p.2202-2215 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals |
| subjects | Degradation E3 ligase F-Box Proteins Fungi Immune response Immunity Kinases Leucine Nicotiana - genetics Nicotiana - microbiology Nicotiana benthamiana pattern‐triggered immunity Phosphotransferases Plant growth Proteasomes Protein Domains Proteins Receptors SCF complex Signal Transduction Ubiquitin Ubiquitin-protein ligase Ubiquitin-Protein Ligases Ubiquitination Xylanase |
| title | An F‐box protein attenuates fungal xylanase‐triggered immunity by destabilizing LRR‐RLP NbEIX2 in a SOBIR1‐dependent manner |
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