Reprogramming of flagellin receptor responses with surrogate ligands
Du-Hwa Lee (),
Ho-Seok Lee,
Min-Soo Choi,
Katarzyna Parys,
Kaori Honda,
Yasumitsu Kondoh,
Jung-Min Lee,
Natalie Edelbacher,
Geon Heo,
Balaji Enugutti,
Hiroyuki Osada,
Ken Shirasu and
Youssef Belkhadir ()
Additional contact information
Du-Hwa Lee: Dr. Bohr-Gasse 3
Ho-Seok Lee: Dr. Bohr-Gasse 3
Min-Soo Choi: Dr. Bohr-Gasse 3
Katarzyna Parys: Dr. Bohr-Gasse 3
Kaori Honda: Wako
Yasumitsu Kondoh: Wako
Jung-Min Lee: Dr. Bohr-Gasse 3
Natalie Edelbacher: Dr. Bohr-Gasse 3
Geon Heo: Dr. Bohr-Gasse 3
Balaji Enugutti: Dr. Bohr-Gasse 3
Hiroyuki Osada: Wako
Ken Shirasu: RIKEN Center for Sustainable Resource Science
Youssef Belkhadir: Dr. Bohr-Gasse 3
Nature Communications, 2024, vol. 15, issue 1, 1-14
Abstract:
Abstract Receptor kinase (RK) families process information from small molecules, short peptides, or glycan ligands to regulate core cellular pathways in plants. To date, whether individual plant RKs are capable of processing signals from distinct types of ligands remains largely unexplored. Addressing this requires the discovery of structurally unrelated ligands that engage the same receptor. Here, we focus on FLAGELLIN-SENSING 2 (FLS2), an RK that senses a peptide of bacterial flagellin to activate antibacterial immunity in Arabidopsis. We interrogate >20,000 potential interactions between small molecules and the sensory domain of FLS2 using a large-scale reverse chemical screen. We discover two small molecules that interact with FLS2 in atypical ways. The surrogate ligands weakly activate the receptor to drive a functional antibacterial response channeled via unusual gene expression programs. Thus, chemical probes acting as biased ligands can be exploited to discover unexpected levels of output flexibility in RKs signal transduction.
Date: 2024
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54271-5
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DOI: 10.1038/s41467-024-54271-5
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