en
Scientific article
Open access
English

Mechanistic basis for the activation of plant membrane receptor kinases by SERK-family coreceptors

Publication date2018
Abstract

Plant-unique membrane receptor kinases with leucine-rich repeat ectodomains (LRR-RKs) can sense small molecule, peptide, and protein ligands. Many LRR-RKs require SERK-family coreceptor kinases for high-affinity ligand binding and receptor activation. How one coreceptor can contribute to the specific binding of distinct ligands and activation of different LRR-RKs is poorly understood. Here we quantitatively analyze the contribution of SERK3 to ligand binding and activation of the brassinosteroid receptor BRI1 and the peptide hormone receptor HAESA. We show that while the isolated receptors sense their respective ligands with drastically different binding affinities, the SERK3 ectodomain binds the ligand-associated receptors with very similar binding kinetics. We identify residues in the SERK3 N-terminal capping domain, which allow for selective steroid and peptide hormone recognition. In contrast, residues in the SERK3 LRR core form a second, constitutive receptor-coreceptor interface. Genetic analyses of protein chimera between BRI1 and SERK3 define that signaling-competent complexes are formed by receptor-coreceptor heteromerization in planta. A functional BRI1-HAESA chimera suggests that the receptor activation mechanism is conserved among different LRR-RKs, and that their signaling specificity is encoded in the kinase domain of the receptor. Our work pinpoints the relative contributions of receptor, ligand, and coreceptor to the formation and activation of SERK-dependent LRR-RK signaling complexes regulating plant growth and development.

Research group
Citation (ISO format)
HOHMANN, Ulrich et al. Mechanistic basis for the activation of plant membrane receptor kinases by SERK-family coreceptors. In: Proceedings of the National Academy of Sciences, 2018. doi: 10.1073/pnas.1714972115
Main files (1)
Article (Published version)
Identifiers
ISSN of the journal0027-8424
488views
196downloads

Technical informations

Creation03/20/2018 7:08:00 PM
First validation03/20/2018 7:08:00 PM
Update time03/15/2023 8:00:06 AM
Status update03/15/2023 8:00:05 AM
Last indexation02/12/2024 12:50:14 PM
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack