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Significance The functional diversity of MAPKs is dependent on differential selection of substrates for phosphorylation. Nevertheless, the mechanisms assisting MAPKs to maintain substrate specificity in plants are not known. Our study shows that WRKY33, a pathogen-responsive MPK3/6 substrate, is SUMOylated in response to pathogen-associated molecular patterns and pathogen signals. SUMOylation mediates WRKY33 phosphorylation and its activation. This correlation is reliant on the selective identification of SUMOylated WRKY33 by MPK3/6 via SUMO interaction motif (SIM) sites. Therefore, WRKY33 SUMOylation is important to selectively interact with MAPKs via the SUMO–SIM module and undergo phosphorylation and thus activation. Our data reveal a mechanism by which MPK3/6 prioritize molecular pathways by differentially selecting substrates using the SUMO–SIM module.

SUMO enables substrate selectivity by mitogen-activated protein kinases to regulate immunity in plants