A putative myristoylated 2C-type protein phosphatase, PP2C74, interacts with SnRK1 in Arabidopsis

N-myristoylation is a lipid modification of many signaling proteins in which myristate is added to an N-terminal glycine residue. Here we show that PP2C74, a putative myristoylated 2C-type protein phosphatase (PP2C) in Arabidopsis, is transcribed in various tissues and has protein phosphatase activity. GFP-fused PP2C74 localized to the plasma membrane, but not when a glycine residue at position 2, which is the putative myristoylation site, was substituted with an alanine residue. Yeast two-hybrid analysis and GST pull-down analysis showed that PP2C74 interacts with AKIN10, the catalytic α subunit of the SnRK1 protein kinase complex, the β subunits of which are known targets of myristoylation.Structured summary of protein interactionsAKIN10physically interacts with PP2C74 by two hybrid (View interaction)AKIN10physically interacts with PP2C74 by pull down (View interaction)

► PP2C74 is expressed in various tissues and has protein phosphatase activity.
► PP2C74 localizes to the plasma membrane in an N-myristoylation-dependent manner.
► PP2C physically interacts with AKIN10, an α subunit of SnRK1.