Abstract
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.
Highlights
Activation of the innate immune system plays an important role in the protection of body surface tissues against microbial invaders
This is in agreement with LYK5 representing the major chitin receptor and inducing chitin signalling through complex formation with CHITIN ELICITOR RECEPTOR KINASE 1 (CERK1) (Cao et al, 2014)
Assuming that S-type anion channels are downstream targets of CERK1-induced guard cell signalling, we tested whether loss of SLOW ANION CHANNEL-ASSOCIATED 1 (SLAC1) or SLAC1 HOMOLOG 3 (SLAH3) would result in impaired chitin-induced stomatal closure
Summary
Activation of the innate immune system plays an important role in the protection of body surface tissues against microbial invaders. Many agronomical important pathogens penetrate plant tissues directly through the epidermis or via stomata (Grimmer et al, 2012; Faulkner and Robatzek, 2012). LysM-domain-containing GLYCOSYLPHOSPHATIDYLINOSITOL (GPI)anchored protein 2 (LYM2) encodes a receptor-like protein predominantly present at plasmodesmal membranes and involved in cell-to-cell signalling (Faulkner et al, 2013). Their ectodomains consist of three LysM domains, of which in CERK1 the middle LysM domain was shown to
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