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

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Version: Final published version
Serval ID
serval:BIB_5DF8F599AFDB
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Mechanistic basis for the activation of plant membrane receptor kinases by SERK-family coreceptors.
Journal
Proceedings of the National Academy of Sciences of the United States of America
Author(s)
Hohmann U., Santiago J., Nicolet J., Olsson V., Spiga F.M., Hothorn L.A., Butenko M.A., Hothorn M.
ISSN
1091-6490 (Electronic)
ISSN-L
0027-8424
Publication state
Published
Issued date
2018
Peer-reviewed
Oui
Volume
115
Number
13
Pages
3488-3493
Language
english
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.
Keywords
brassinosteroid signaling, floral abscission, leucine-rich repeat domain, membrane receptor kinase, receptor activation
Pubmed
Web of science
Open Access
Yes
Create date
16/05/2018 12:56
Last modification date
20/08/2019 14:16
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