Format

Send to

Choose Destination
Nature. 2018 Jan 18;553(7688):342-346. doi: 10.1038/nature25184. Epub 2018 Jan 10.

An extracellular network of Arabidopsis leucine-rich repeat receptor kinases.

Author information

1
Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna Biocenter (VBC), Dr Bohr-Gasse 3, 1030 Vienna, Austria.
2
Department of Cell & Systems Biology, University of Toronto, 25 Willcocks St., Toronto, Ontario, Canada.
3
The Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, UK.
4
Department of Biology, University of Alabama at Birmingham, Birmingham, Alabama, USA.
5
Protein Technologies Facility, Vienna Biocenter Core Facilities (VBCF), Vienna, Austria.
6
Salk Institute for Biological Studies, Plant Molecular and Cellular Biology Laboratory, 10010 N Torrey Pines Rd, La Jolla, California 92037, USA.
7
Research Institute of Molecular Pathology (IMP), Vienna Biocenter (VBC), Campus-Vienna-Biocenter 1, 1030 Vienna, Austria.
8
Institute of Molecular Biotechnology GmbH (IMBA), Vienna Biocenter (VBC), Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
9
Centre for the Analysis of Genome Evolution & Function, 25 Willcocks St., University of Toronto, Toronto, Ontario, Canada.

Abstract

The cells of multicellular organisms receive extracellular signals using surface receptors. The extracellular domains (ECDs) of cell surface receptors function as interaction platforms, and as regulatory modules of receptor activation. Understanding how interactions between ECDs produce signal-competent receptor complexes is challenging because of their low biochemical tractability. In plants, the discovery of ECD interactions is complicated by the massive expansion of receptor families, which creates tremendous potential for changeover in receptor interactions. The largest of these families in Arabidopsis thaliana consists of 225 evolutionarily related leucine-rich repeat receptor kinases (LRR-RKs), which function in the sensing of microorganisms, cell expansion, stomata development and stem-cell maintenance. Although the principles that govern LRR-RK signalling activation are emerging, the systems-level organization of this family of proteins is unknown. Here, to address this, we investigated 40,000 potential ECD interactions using a sensitized high-throughput interaction assay, and produced an LRR-based cell surface interaction network (CSILRR) that consists of 567 interactions. To demonstrate the power of CSILRR for detecting biologically relevant interactions, we predicted and validated the functions of uncharacterized LRR-RKs in plant growth and immunity. In addition, we show that CSILRR operates as a unified regulatory network in which the LRR-RKs most crucial for its overall structure are required to prevent the aberrant signalling of receptors that are several network-steps away. Thus, plants have evolved LRR-RK networks to process extracellular signals into carefully balanced responses.

PMID:
29320478
DOI:
10.1038/nature25184
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Nature Publishing Group
Loading ...
Support Center