ArticleScience advances2025
Reciprocal phosphorylation between SOAK1 and SOBIR1 fine-tunes receptor-like protein (RLP)-mediated plant immunity.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Multiple BnaSOBIR1-Associated Receptor-like Proteins Contribute to Enhanced Resistance toPlants (Basel, Switzerland) · 2026Article
- A Virus-Inducible E3-RLCK-MADS Module Coordinates Suppression of Plant Immunity and Fertility in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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