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An extracellular network of Arabidopsis leucine-rich repeat receptor kinases.
- Source :
-
Nature [Nature] 2018 Jan 18; Vol. 553 (7688), pp. 342-346. Date of Electronic Publication: 2018 Jan 10. - Publication Year :
- 2018
-
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 (CSI <superscript>LRR</superscript> ) that consists of 567 interactions. To demonstrate the power of CSI <superscript>LRR</superscript> 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 CSI <superscript>LRR</superscript> 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.
- Subjects :
- Arabidopsis cytology
Arabidopsis immunology
Arabidopsis microbiology
Protein Binding
Protein Domains
Protein Serine-Threonine Kinases chemistry
Protein Serine-Threonine Kinases metabolism
Receptors, Cell Surface chemistry
Receptors, Cell Surface metabolism
Reproducibility of Results
Signal Transduction
Arabidopsis enzymology
Arabidopsis Proteins chemistry
Arabidopsis Proteins metabolism
Leucine metabolism
Protein Kinases chemistry
Protein Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1476-4687
- Volume :
- 553
- Issue :
- 7688
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 29320478
- Full Text :
- https://doi.org/10.1038/nature25184