Reciprocal phosphorylation between SOAK1 and SOBIR1 fine-tunes receptor-like protein (RLP)-mediated plant immunity.

Abstract

SUPPRESSOR OF BIR1-1 (SOBIR1) is a receptor-like kinase (RLK) that acts as a coreceptor for multiple receptor-like proteins (RLPs) to mediate pathogen-associated molecular pattern)-triggered immunity. However, the regulation of SOBIR1 homeostasis and activity remains largely unknown. Our study reveals that SOBIR1-ASSOCIATED PROTEIN KINASE 1 (SOAK1), a member of the receptor-like cytoplasmic kinase (RLCK)-V subfamily with a transmembrane domain, negatively regulates multiple RLP-mediated immune responses. SOAK1 constitutively interacts with SOBIR1 and modulates SOBIR1-dependent immune signaling. SOAK1 directly phosphorylates SOBIR1 at serine-406, substantially impairing its ability to transphosphorylate itself and BAK1. The conservation of serine-406 residue among various flowering plants suggests that phosphorylation at this site plays a critical role in regulating plant immunity. Conversely, SOBIR1 also phosphorylates SOAK1 primarily at serine-73, inhibiting SOAK1's kinase activity and derepressing SOBIR1 activity. This study elucidates a regulatory mechanism for SOBIR1 activity and highlights an uncharacterized role of RLCK-V subfamily members in plant immunity.