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We have established the novel interaction between mCHL2, Tsg and BMP-2 for the first time. Tsg binds to VWC1 and VWC3 of mCHL2 in a cooperative waz and plazs a role in strengthening the binding affinity. Furthermore, Tsg/mCHL2/BMP-2 termary complex and Tsg/mCHL2 binary complex have been isolated by gel-filtration chromatography. Therefore mCHL2 can form a ternary complex with Tsg and BMP-2 and this complex makes mCHL2 a better BMP-2 antagnonist.
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.