Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure
In plants, antimicrobial immune responses involve the cellular release of anions and are responsible for the closure of stomatal pores. Detection of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) induces currents mediated via slow-type (S-type) anion channels b...
| Main Authors: | , , , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2019-09-01
|
| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/44474 |
| _version_ | 1811252953193906176 |
|---|---|
| author | Yi Liu Tobias Maierhofer Katarzyna Rybak Jan Sklenar Andy Breakspear Matthew G Johnston Judith Fliegmann Shouguang Huang M Rob G Roelfsema Georg Felix Christine Faulkner Frank LH Menke Dietmar Geiger Rainer Hedrich Silke Robatzek |
| author_facet | Yi Liu Tobias Maierhofer Katarzyna Rybak Jan Sklenar Andy Breakspear Matthew G Johnston Judith Fliegmann Shouguang Huang M Rob G Roelfsema Georg Felix Christine Faulkner Frank LH Menke Dietmar Geiger Rainer Hedrich Silke Robatzek |
| author_sort | Yi Liu |
| collection | DOAJ |
| description | In plants, antimicrobial immune responses involve the cellular release of anions and are responsible for the closure of stomatal pores. Detection of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) induces currents mediated via slow-type (S-type) anion channels by a yet not understood mechanism. Here, we show that stomatal closure to fungal chitin is conferred by the major PRRs for chitin recognition, LYK5 and CERK1, the receptor-like cytoplasmic kinase PBL27, and the SLAH3 anion channel. PBL27 has the capacity to phosphorylate SLAH3, of which S127 and S189 are required to activate SLAH3. Full activation of the channel entails CERK1, depending on PBL27. Importantly, both S127 and S189 residues of SLAH3 are required for chitin-induced stomatal closure and anti-fungal immunity at the whole leaf level. Our results demonstrate a short signal transduction module from MAMP recognition to anion channel activation, and independent of ABA-induced SLAH3 activation. |
| first_indexed | 2024-04-12T16:43:33Z |
| format | Article |
| id | doaj.art-af364255b6b34549b1e25b874cab5474 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T16:43:33Z |
| publishDate | 2019-09-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-af364255b6b34549b1e25b874cab54742022-12-22T03:24:41ZengeLife Sciences Publications LtdeLife2050-084X2019-09-01810.7554/eLife.44474Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closureYi Liu0Tobias Maierhofer1Katarzyna Rybak2Jan Sklenar3Andy Breakspear4Matthew G Johnston5https://orcid.org/0000-0003-1141-6135Judith Fliegmann6Shouguang Huang7M Rob G Roelfsema8Georg Felix9Christine Faulkner10https://orcid.org/0000-0003-3905-8077Frank LH Menke11https://orcid.org/0000-0003-2490-4824Dietmar Geiger12https://orcid.org/0000-0003-0715-5710Rainer Hedrich13https://orcid.org/0000-0003-3224-1362Silke Robatzek14https://orcid.org/0000-0002-9788-322XThe Sainsbury Laboratory, Norwich, United KingdomInstitute for Molecular Plant Physiology and Biophysics, Julius-von-Sachs-Institute, Biocenter, University of Wuerzburg, Wuerzburg, GermanyLMU Biocenter, Ludwig-Maximilian-University of Munich, Martinsried, GermanyThe Sainsbury Laboratory, Norwich, United KingdomJohn Innes Centre, Norwich, United KingdomJohn Innes Centre, Norwich, United KingdomDepartment of Plant Biochemistry, Center for Plant Molecular Biology (ZMBP), University of Tuebingen, Tuebingen, GermanyInstitute for Molecular Plant Physiology and Biophysics, Julius-von-Sachs-Institute, Biocenter, University of Wuerzburg, Wuerzburg, GermanyInstitute for Molecular Plant Physiology and Biophysics, Julius-von-Sachs-Institute, Biocenter, University of Wuerzburg, Wuerzburg, GermanyDepartment of Plant Biochemistry, Center for Plant Molecular Biology (ZMBP), University of Tuebingen, Tuebingen, GermanyJohn Innes Centre, Norwich, United KingdomThe Sainsbury Laboratory, Norwich, United KingdomInstitute for Molecular Plant Physiology and Biophysics, Julius-von-Sachs-Institute, Biocenter, University of Wuerzburg, Wuerzburg, GermanyInstitute for Molecular Plant Physiology and Biophysics, Julius-von-Sachs-Institute, Biocenter, University of Wuerzburg, Wuerzburg, GermanyThe Sainsbury Laboratory, Norwich, United Kingdom; LMU Biocenter, Ludwig-Maximilian-University of Munich, Martinsried, GermanyIn plants, antimicrobial immune responses involve the cellular release of anions and are responsible for the closure of stomatal pores. Detection of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) induces currents mediated via slow-type (S-type) anion channels by a yet not understood mechanism. Here, we show that stomatal closure to fungal chitin is conferred by the major PRRs for chitin recognition, LYK5 and CERK1, the receptor-like cytoplasmic kinase PBL27, and the SLAH3 anion channel. PBL27 has the capacity to phosphorylate SLAH3, of which S127 and S189 are required to activate SLAH3. Full activation of the channel entails CERK1, depending on PBL27. Importantly, both S127 and S189 residues of SLAH3 are required for chitin-induced stomatal closure and anti-fungal immunity at the whole leaf level. Our results demonstrate a short signal transduction module from MAMP recognition to anion channel activation, and independent of ABA-induced SLAH3 activation.https://elifesciences.org/articles/44474MAMPPAMP-triggered immunityPTICERK1LYK5SLAH3 |
| spellingShingle | Yi Liu Tobias Maierhofer Katarzyna Rybak Jan Sklenar Andy Breakspear Matthew G Johnston Judith Fliegmann Shouguang Huang M Rob G Roelfsema Georg Felix Christine Faulkner Frank LH Menke Dietmar Geiger Rainer Hedrich Silke Robatzek Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure eLife MAMP PAMP-triggered immunity PTI CERK1 LYK5 SLAH3 |
| title | Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure |
| title_full | Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure |
| title_fullStr | Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure |
| title_full_unstemmed | Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure |
| title_short | Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure |
| title_sort | anion channel slah3 is a regulatory target of chitin receptor associated kinase pbl27 in microbial stomatal closure |
| topic | MAMP PAMP-triggered immunity PTI CERK1 LYK5 SLAH3 |
| url | https://elifesciences.org/articles/44474 |
| work_keys_str_mv | AT yiliu anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT tobiasmaierhofer anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT katarzynarybak anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT jansklenar anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT andybreakspear anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT matthewgjohnston anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT judithfliegmann anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT shouguanghuang anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT mrobgroelfsema anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT georgfelix anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT christinefaulkner anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT franklhmenke anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT dietmargeiger anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT rainerhedrich anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure AT silkerobatzek anionchannelslah3isaregulatorytargetofchitinreceptorassociatedkinasepbl27inmicrobialstomatalclosure |