Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure

eLife

Georg Felix¹  Judith Fliegmann¹  M Rob G Roelfsema²  Tobias Maierhofer²  Shouguang Huang²  Rainer Hedrich²  Dietmar Geiger²  Andy Breakspear³  Matthew G Johnston³  Christine Faulkner³  Katarzyna Rybak⁴  Silke Robatzek⁵  Frank LH Menke⁵  Yi Liu⁵  Jan Sklenar⁵ 

[1] Department of Plant Biochemistry, Center for Plant Molecular Biology (ZMBP), University of Tuebingen, Tuebingen, Germany;Institute for Molecular Plant Physiology and Biophysics, Julius-von-Sachs-Institute, Biocenter, University of Wuerzburg, Wuerzburg, Germany;John Innes Centre, Norwich, United Kingdom;LMU Biocenter, Ludwig-Maximilian-University of Munich, Martinsried, Germany;The Sainsbury Laboratory, Norwich, United Kingdom;

关键词: MAMP;    PAMP-triggered immunity;    PTI;    CERK1;    LYK5;    SLAH3;   

DOI  :  10.7554/eLife.44474

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown