Abstract
Plant genomes encode hundreds of receptor-like kinases (RLKs) with an organization of functional domains similar to those of animal receptor kinases. Ligand-dependent phosphorylation has now been demonstrated for several plant RLKs and identification of specific phosphorylation sites followed by their functional characterization has advanced our understanding of RLK signaling mechanisms regulating growth, morphogenesis, and disease resistance. Advances in mass spectrometry and phosphopeptide enrichment technology have been applied to plant phosphoproteomics, revealing hundreds of novel in vivo RLK phosphorylation sites and allowing comparative analysis of phosphorylation site sequence motifs. This chapter examines recent studies on both targeted RLK phosphorylation site analysis and global phosphoproteomic studies that have generated data useful for understanding mechanisms of RLK phosphorylation and its role in plant signal transduction.
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Clouse, S.D., Goshe, M.B., Huber, S.C. (2012). Phosphorylation and RLK Signaling. In: Tax, F., Kemmerling, B. (eds) Receptor-like Kinases in Plants. Signaling and Communication in Plants, vol 13. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-23044-8_12
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