Plant pattern recognition receptor complexes at the plasma membrane
► Plant PRRs are surface-localized RLKs or RLPs that form multi-protein complexes. ► The LRR-RLK BAK1 is a major regulator of several PRR-mediated pathways. ► The LysM-RLK CERK1 is part of multi-specificity recognition complexes. ► The cytoplasmic kinase BIK1 is a key regulator of PTI downstream of...
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Veröffentlicht in: | Current opinion in plant biology 2012-08, Vol.15 (4), p.349-357 |
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description | ► Plant PRRs are surface-localized RLKs or RLPs that form multi-protein complexes. ► The LRR-RLK BAK1 is a major regulator of several PRR-mediated pathways. ► The LysM-RLK CERK1 is part of multi-specificity recognition complexes. ► The cytoplasmic kinase BIK1 is a key regulator of PTI downstream of multiple PRRs. ► Phosphorylation and ubiquitination events regulate the activity of PRR complexes.
A key feature of innate immunity is the ability to recognize and respond to potential pathogens in a highly sensitive and specific manner. In plants, the activation of pattern recognition receptors (PRRs) by pathogen-associated molecular patterns (PAMPs) elicits a defense programme known as PAMP-triggered immunity (PTI). Although only a handful of PAMP-PRR pairs have been defined, all known PRRs are modular transmembrane proteins containing ligand-binding ectodomains. It is becoming clear that PRRs do not act alone but rather function as part of multi-protein complexes at the plasma membrane. Recent studies describing the molecular interactions and protein modifications that occur between PRRs and their regulatory proteins have provided important mechanistic insight into how plants avoid infection and achieve immunity. |
doi_str_mv | 10.1016/j.pbi.2012.05.006 |
format | Article |
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A key feature of innate immunity is the ability to recognize and respond to potential pathogens in a highly sensitive and specific manner. In plants, the activation of pattern recognition receptors (PRRs) by pathogen-associated molecular patterns (PAMPs) elicits a defense programme known as PAMP-triggered immunity (PTI). Although only a handful of PAMP-PRR pairs have been defined, all known PRRs are modular transmembrane proteins containing ligand-binding ectodomains. It is becoming clear that PRRs do not act alone but rather function as part of multi-protein complexes at the plasma membrane. Recent studies describing the molecular interactions and protein modifications that occur between PRRs and their regulatory proteins have provided important mechanistic insight into how plants avoid infection and achieve immunity.</description><identifier>ISSN: 1369-5266</identifier><identifier>EISSN: 1879-0356</identifier><identifier>DOI: 10.1016/j.pbi.2012.05.006</identifier><identifier>PMID: 22705024</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Cell Membrane - metabolism ; Disease Resistance - immunology ; Host-Pathogen Interactions ; immunity ; Indexing in process ; Membrane Proteins - metabolism ; pathogens ; Plant Diseases - immunology ; Plant Immunity - immunology ; Plants - metabolism ; Plants - microbiology ; plasma membrane ; receptors ; Receptors, Pattern Recognition - metabolism ; regulatory proteins ; Signal Transduction ; transmembrane proteins</subject><ispartof>Current opinion in plant biology, 2012-08, Vol.15 (4), p.349-357</ispartof><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c476t-60198701b5d8ec4083f8526119325a8db92fc5fcbabeabb83529a4ad894d9ade3</citedby><cites>FETCH-LOGICAL-c476t-60198701b5d8ec4083f8526119325a8db92fc5fcbabeabb83529a4ad894d9ade3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1369526612000878$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22705024$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Monaghan, Jacqueline</creatorcontrib><creatorcontrib>Zipfel, Cyril</creatorcontrib><title>Plant pattern recognition receptor complexes at the plasma membrane</title><title>Current opinion in plant biology</title><addtitle>Curr Opin Plant Biol</addtitle><description>► Plant PRRs are surface-localized RLKs or RLPs that form multi-protein complexes. ► The LRR-RLK BAK1 is a major regulator of several PRR-mediated pathways. ► The LysM-RLK CERK1 is part of multi-specificity recognition complexes. ► The cytoplasmic kinase BIK1 is a key regulator of PTI downstream of multiple PRRs. ► Phosphorylation and ubiquitination events regulate the activity of PRR complexes.
A key feature of innate immunity is the ability to recognize and respond to potential pathogens in a highly sensitive and specific manner. In plants, the activation of pattern recognition receptors (PRRs) by pathogen-associated molecular patterns (PAMPs) elicits a defense programme known as PAMP-triggered immunity (PTI). Although only a handful of PAMP-PRR pairs have been defined, all known PRRs are modular transmembrane proteins containing ligand-binding ectodomains. It is becoming clear that PRRs do not act alone but rather function as part of multi-protein complexes at the plasma membrane. Recent studies describing the molecular interactions and protein modifications that occur between PRRs and their regulatory proteins have provided important mechanistic insight into how plants avoid infection and achieve immunity.</description><subject>Cell Membrane - metabolism</subject><subject>Disease Resistance - immunology</subject><subject>Host-Pathogen Interactions</subject><subject>immunity</subject><subject>Indexing in process</subject><subject>Membrane Proteins - metabolism</subject><subject>pathogens</subject><subject>Plant Diseases - immunology</subject><subject>Plant Immunity - immunology</subject><subject>Plants - metabolism</subject><subject>Plants - microbiology</subject><subject>plasma membrane</subject><subject>receptors</subject><subject>Receptors, Pattern Recognition - metabolism</subject><subject>regulatory proteins</subject><subject>Signal Transduction</subject><subject>transmembrane proteins</subject><issn>1369-5266</issn><issn>1879-0356</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0Eoh_wA7jQHHtJGNux44gTWvVLqgQS9GzZzqR4lcSp7a3g3-Ptlh7hNHN45p3xY0I-UGgoUPlp26zWNwwoa0A0APIVOaaq62vgQr4uPZd9LZiUR-QkpS0ACNbxt-SIsQ4EsPaYbL5NZsnVanLGuFQRXbhffPbhqcc1h1i5MK8T_sJUmVzln1itk0mzqWacbTQLviNvRjMlfP9cT8nd5cWPzXV9-_XqZvPltnZtJ3MtgfaqA2rFoNC1oPioynGU9pwJowbbs9GJ0Vlj0ViruGC9ac2g-nbozYD8lJwfctcYHnaYsp59cjiVF2DYJU0Zo5QrIeD_KPCyGbonlB5QF0NKEUe9Rj-b-LtAeq9Zb3XRrPeaNQhdNJeZj8_xOzvj8DLx12sBzg7AaII299Enffe9JLT7P2ilEIX4fCCwGHv0GHVyHheHgy_isx6C_8cBfwBvPpX7</recordid><startdate>20120801</startdate><enddate>20120801</enddate><creator>Monaghan, Jacqueline</creator><creator>Zipfel, Cyril</creator><general>Elsevier Ltd</general><scope>FBQ</scope><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>7X8</scope><scope>F1W</scope><scope>H98</scope><scope>L.G</scope></search><sort><creationdate>20120801</creationdate><title>Plant pattern recognition receptor complexes at the plasma membrane</title><author>Monaghan, Jacqueline ; Zipfel, Cyril</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c476t-60198701b5d8ec4083f8526119325a8db92fc5fcbabeabb83529a4ad894d9ade3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Cell Membrane - metabolism</topic><topic>Disease Resistance - immunology</topic><topic>Host-Pathogen Interactions</topic><topic>immunity</topic><topic>Indexing in process</topic><topic>Membrane Proteins - metabolism</topic><topic>pathogens</topic><topic>Plant Diseases - immunology</topic><topic>Plant Immunity - immunology</topic><topic>Plants - metabolism</topic><topic>Plants - microbiology</topic><topic>plasma membrane</topic><topic>receptors</topic><topic>Receptors, Pattern Recognition - metabolism</topic><topic>regulatory proteins</topic><topic>Signal Transduction</topic><topic>transmembrane proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Monaghan, Jacqueline</creatorcontrib><creatorcontrib>Zipfel, Cyril</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><jtitle>Current opinion in plant biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Monaghan, Jacqueline</au><au>Zipfel, Cyril</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Plant pattern recognition receptor complexes at the plasma membrane</atitle><jtitle>Current opinion in plant biology</jtitle><addtitle>Curr Opin Plant Biol</addtitle><date>2012-08-01</date><risdate>2012</risdate><volume>15</volume><issue>4</issue><spage>349</spage><epage>357</epage><pages>349-357</pages><issn>1369-5266</issn><eissn>1879-0356</eissn><abstract>► Plant PRRs are surface-localized RLKs or RLPs that form multi-protein complexes. ► The LRR-RLK BAK1 is a major regulator of several PRR-mediated pathways. ► The LysM-RLK CERK1 is part of multi-specificity recognition complexes. ► The cytoplasmic kinase BIK1 is a key regulator of PTI downstream of multiple PRRs. ► Phosphorylation and ubiquitination events regulate the activity of PRR complexes.
A key feature of innate immunity is the ability to recognize and respond to potential pathogens in a highly sensitive and specific manner. In plants, the activation of pattern recognition receptors (PRRs) by pathogen-associated molecular patterns (PAMPs) elicits a defense programme known as PAMP-triggered immunity (PTI). Although only a handful of PAMP-PRR pairs have been defined, all known PRRs are modular transmembrane proteins containing ligand-binding ectodomains. It is becoming clear that PRRs do not act alone but rather function as part of multi-protein complexes at the plasma membrane. Recent studies describing the molecular interactions and protein modifications that occur between PRRs and their regulatory proteins have provided important mechanistic insight into how plants avoid infection and achieve immunity.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>22705024</pmid><doi>10.1016/j.pbi.2012.05.006</doi><tpages>9</tpages></addata></record> |
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subjects | Cell Membrane - metabolism Disease Resistance - immunology Host-Pathogen Interactions immunity Indexing in process Membrane Proteins - metabolism pathogens Plant Diseases - immunology Plant Immunity - immunology Plants - metabolism Plants - microbiology plasma membrane receptors Receptors, Pattern Recognition - metabolism regulatory proteins Signal Transduction transmembrane proteins |
title | Plant pattern recognition receptor complexes at the plasma membrane |
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