The SERK family as co-receptors for FLS2
P. CHATELAIN (1), M. Albert (1), U. Fürst (1), G. Felix (1) (1) ZMBP - Center for Plant Molecular Biology, Tuebingen University, Germany

Flg22 from bacterial flagellin is recognized by the FLAGELLIN-SENSITIVE 2 (FLS2) receptor. Upon ligand binding, FLS2 forms a heteromeric complex with SERK3/BAK1, initiating the signaling cascade which then leads to PTI. Previous studies reported that FLS2 showed residual signaling in serk3 mutant plants [1]. The SERK family comprises four other members, with high sequence similarity and with potential functional redundancy. Since mutants with defects in multiple SERKs are lethal, we used the two-hybrid-receptor approach to test functionality of the individual SERKs in mediating the flg22-induced FLS2 response. Transient co-expression of the chimeric receptor pairs, FLS2 and SERK with swapped cytoplasmic domains, in protoplasts of Arabidopsis fls2 bak1-4 double mutants showed that SERK1, SERK2, SERK4 but not SERK5 ectodomains can act as co-receptors for FLS2, yet with different efficiencies. Further constructs with specific alterations in the extracellular domains of the SERKs were tested to pin down the residues important for high efficiency of flg22 signaling. Genomic Screens to Identify Next-Generation MAMPs and their Cognate Pattern Recognition Receptors    

Abstract Number: P17-507
Session Type: Poster