Investigation of Autophosphorylation Sites of Plant Receptor Kinases and Phosphorylation of Interacting Partners.

ABSTRACT

The optimal kinase activity of plant receptor-like kinases (RLKs) is often regulated by autophosphorylation of specific sites. Many of these phosphorylated residues then serve as recruiting sites for downstream interacting proteins. Therefore, identification of the phosphosites can be an important first step in delineating the signaling network. This chapter describes a protocol for identification of phosphorylated residues by mass spectrometry as well as a protocol to determine if an interacting partner can be phosphorylated in vitro.