Recent advances in proteomics, MS analysis, and high-throughput cloning have facilitated a global comparative analysis of biochemical function of the entire LRR RLK family in Arabidopsis. The genetic resources and completed genomic sequence of this model plant, coupled with increased sensitivity of LC-MS/MS approaches and reliable quantitative methods for following phosphorylation status at specific residues in vivo, will allow building of a comprehensive database of LRR RLK phosphorylation sites as well as analyzing the biological significance of these phosphorylation events. Over the next five years we plan to significantly increase the number of LRR RLKs included in this database, which should enhance our understanding of the molecular mechanisms involved in the control of plant growth and development by LRR RLKs. This family-wide analysis of the biochemical properties of LRR RLK kinase domains may also show whether differential kinase activity, autophosphorylation sites, and substrate preferences will allow a grouping of kinases that correlates with the phylo-genetic arrangement of subfamily categories determined by kinase domain sequence alignment. The LRR motif is thought to be involved in PPIs, and it would not be surprising if many LRR RLKs formed a variety of heterodimers among family members, which might be essential for signaling responses to different ligands. Thus, a tool set of LRR RLK clones with different epitope tags will be useful for interaction studies both in vitro and in vivo. Characterization of the BRI1/BAK1 model system has shown that plant receptor kinases share the general paradigm of animal receptor kinase function, including ligand-dependent heterodimerization and phosphorylation on specific residues of the cytoplasmic kinase domain. We plan to expand the BRI1/BAK1 approach to other LRR RLKs of both known and unknown function to increase our understanding of this large family of critical signaling proteins.
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