Leucine-rich repeat receptor-like kinase II phylogenetics reveals five main clades throughout the plant kingdom.

Receptor-like kinases (RLKs) represent the largest group of cell surface receptors in plants. The monophyletic leucine-rich repeat (LRR)-RLK subfamily II is considered to contain the somatic embryogenesis receptor kinases (SERKs) and NSP-interacting kinases known to be involved in developmental processes and cellular immunity in plants. There are only a few published studies on the phylogenetics of LRR-RLKII; unfortunately these suffer from poor taxon/gene sampling. Hence, it is not clear how many and what main clades this family contains, let alone what structure-function relationships exist. We used 1342 protein sequences annotated as 'SERK' and 'SERK-like' plus related sequences in order to estimate phylogeny within the LRR-RLKII clade, using the nematode protein kinase Pelle as an outgroup. We reconstruct five main clades (LRR-RLKII 1-5), in each of which the main pattern of land plant relationships re-occurs, confirming previous hypotheses that duplication events happened in this gene subfamily prior to divergence among land plant lineages. We show that domain structures and intron-exon boundaries within the five clades are well conserved in evolution. Furthermore, phylogenetic patterns based on the separate LRR and kinase parts of LRR-RLKs are incongruent: whereas the LRR part supports a LRR-RLKII 2/3 sister group relationship, the kinase part supports clades 1/2. We infer that the kinase part includes few 'radical' amino acid changes compared with the LRR part. Finally, our results confirm that amino acids involved in each LRR-RLKII-receptor complex interaction are located at N-capping residues, and that the short amino acid motifs of this interaction domain are highly conserved throughout evolution within the five LRR-RLKII clades.