@article {Hind529172, author = {Sarah R. Hind and Robyn Roberts and Kerry F. Pedley and Benjamin A. Diner and Matthew J. Szarzanowicz and Dianiris Luciano-Rosario and Bharat B. Majhi and Georgy Popov and Guido Sessa and Chang-Sik Oh and Gregory B. Martin}, title = {Mai1 protein acts between host recognition of pathogen effectors and MAPK signaling}, elocation-id = {529172}, year = {2019}, doi = {10.1101/529172}, publisher = {Cold Spring Harbor Laboratory}, abstract = {The molecular mechanisms acting between host recognition of pathogen effectors by NOD-like receptor (NLR) proteins and mitogen-activated protein kinase (MAPK) signaling cascades are unknown. MAPKKKα (M3Kα) activates MAPK signaling leading to programmed cell death (PCD) associated with NLR-triggered immunity. We identified a tomato M3Kα-interacting protein, SlMai1, that has 80\% amino acid identity with Arabidopsis brassinosteroid kinase 1 (AtBsk1). SlMai1 has a protein kinase domain and a C-terminal tetratricopeptide repeat domain which interacts with the kinase domain of M3Kα. Virus-induced gene silencing of Mai1 homologs in Nicotiana benthamiana increased susceptibility to Pseudomonas syringae and compromised PCD induced by four NLR proteins. PCD was restored by expression of a synthetic SlMai1 gene that resists silencing. Expression of AtBsk1 did not restore PCD in Mai1-silenced plants, suggesting SlMai1 is functionally divergent from AtBsk1. PCD caused by overexpression of M3Kα or MKK2 was unaffected by Mai1 silencing indicating Mai1 acts upstream of these proteins. Co-expression of Mai1 with M3Kα in leaves enhanced MAPK phosphorylation and accelerated PCD. These findings reveal Mai1 as a molecular link acting between host recognition of pathogens and MAPK signaling.Author Summary Plants use intracellular immune receptors to detect and respond to specific effector proteins which pathogens translocate into the host cell as part of their infection process. Localized programmed cell death (PCD) involving a mitogen-activated protein kinase (MAPK) cascade is an important host response associated with effector-triggered immunity, although the molecular connections between immune receptors and MAPK signaling is unknown. The Mai1 protein was found to act downstream of multiple immune receptors in Nicotiana benthamiana and to physically interact with MAPKKKα. The Mai1-MAPKKKα interaction enhances MAPK phosphorylation, triggers PCD and promotes disease resistance.}, URL = {https://www.biorxiv.org/content/early/2019/01/23/529172}, eprint = {https://www.biorxiv.org/content/early/2019/01/23/529172.full.pdf}, journal = {bioRxiv} }