Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 20, Pages 8503-8507Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1103556108
Keywords
brassinosteroid signaling; flagellin signaling; plant innate immunity; Receptor-like kinase; signaling crosstalk
Categories
Funding
- Howard Hughes Medical Institute
- National Science Foundation [IOS-0649389, IOS-0929410]
- National Institutes of Health [GM057171, GM066025]
- Philippe Foundation
- European Molecular Biology Organization
- Marc and Eva Stern Foundation
- CAPES (Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior)
- CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnologico)
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Receptor kinases with leucine-rich repeat (LRR) extracellular domains form the largest family of receptors in plants. In the few cases for which there is mechanistic information, ligand binding in the extracellular domain often triggers the recruitment of a LRR-coreceptor kinase. The current model proposes that this recruitment is mediated by their respective kinase domains. Here, we show that the extracellular LRR domain of BRI1-ASSOCIATED KINASE1 (BAK1), a coreceptor involved in the disparate processes of cell surface steroid signaling and immunity in plants, is critical for its association with specific ligand-binding LRR-containing receptors. The LRRs of BAK1 thus serve as a platform for the molecular assembly of signal-competent receptors. We propose that this mechanism represents a paradigm for LRR receptor activation in plants.
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