Chemical control of receptor kinase signaling by rapamycin-induced dimerization

Sara Kim, Jeonghyang Park, Byeong Wook Jeon, Geonhee Hwang, Na Young Kang, Yeim We, Won Young Park, Eunkyoo Oh, Jungmook Kim

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


Membrane-localized leucine-rich repeat receptor kinases (LRR-RKs) sense diverse extracellular signals, and coordinate and specify cellular functions in plants. However, functional understanding and identification of the cellular signaling of most LRR-RKs remain a major challenge owing to their genetic redundancy, the lack of ligand information, and subtle phenotypes of LRR-RK overexpression. Here, we report an engineered rapamycin-inducible dimerization (RiD) receptor system that triggers a receptor-specific LRR-RK signaling independent of their cognate ligands or endogenous receptors. Using the RiD-receptors, we demonstrated that the rapamycin-mediated association of chimeric cytosolic kinase domains from the BRI1/BAK1 receptor/co-receptor, but not the BRI1/BRI1 or BAK1/BAK1 homodimer, is sufficient to activate downstream brassinosteroid signaling and physiological responses. Furthermore, we showed that the engineered RiD-FLS2/BAK1 could activate flagellin-22-mediated immune signaling and responses. Using the RiD system, we also identified the potential function of an unknown orphan receptor in immune signaling and revealed the differential activities of SERK co-receptors of LRR-RKs. Our results indicate that the RiD method can serve as a synthetic biology tool for precise temporal manipulation of LRR-RK signaling and for understanding LRR-RK biology.

Original languageEnglish
Pages (from-to)1379-1390
Number of pages12
JournalMolecular Plant
Issue number8
Publication statusPublished - 2021 Aug 2


  • BAK1
  • BRI1
  • FLS2
  • brassinosteroids
  • leucine-rich repeat receptor kinase

ASJC Scopus subject areas

  • Molecular Biology
  • Plant Science


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