TY  - JOUR
A1  - Liu, Yi
A1  - Maierhofer, Tobias
A1  - Rybak, Katarzyna
A1  - Sklenar, Jan
A1  - Breakspear, Andy
A1  - Johnston, Matthew G.
A1  - Fliegmann, Judith
A1  - Huang, Shouguang
A1  - Roelfsema, M. Rob G.
A1  - Felix, Georg
A1  - Faulkner, Christine
A1  - Menke, Frank L.H.
A1  - Geiger, Dietmar
A1  - Hedrich, Rainer
A1  - Robatzek, Silke
T1  - Anion channel SLAH3 is a regulatory target of chitin receptor-associated kinase PBL27 in microbial stomatal closure
JF  - eLife
N2  - 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.
KW  - plants
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-202631
VL  - 8
ER  -