Phosphorylation of Movement Proteins by the Plasmodesmal-Associated Protein Kinase

Plant viruses encode movement proteins (MPs) which play important roles in spreading their infectious materials throughout host plants. This infection is facilitated by cell-to-cell trafficking of MPs through specialized channels termed plasmodesmata, which involves specific interactions between MPs and host factors. Recently, we have reported the identification of a host protein kinase named plasmodesmal-associated protein kinase (PAPK) which specifically phosphorylates a subset of noncell autonomous proteins in vitro, including MPs of Tobacco mosaic virus (TMV) and Bean dwarf mosaic virus (BDMV). Biochemical purification of PAPK was achieved by developing a method in which a series of liquid chroma-tographic separations of plasmodesmal-enriched subcellular fractions was coupled with phosphorylation assays using TMV MP as a substrate. Application of this approach may prove useful in isolating other host kinases that interact with various viral components.