PPA2A dephosphorylates SPRY2 Authored: Rothfels, K, 2011-08-15 In unstimulated cells, SPRY2 has been shown to be phosphorylated on multiple serine and threonine residues. In these cells, SPRY2 exists in a complex with the regulatory and catalytic subunits (A and C, respectively) of the serine/threonine phosphatase PP2A. After stimulation with FGF, the catalytic activity of PP2A increases and the phosphatase dephophorylates SPRY at serine 112 and serine 115. This is thought to promote changes in tertiary structure that promote GRB2 binding and phosphorylation of Y55 and Y227. Pubmed17255109 Reactome Database ID Release 431295632 Reactome, http://www.reactome.org ReactomeREACT_111094 Reviewed: Gotoh, N, 2011-08-26 has a Stoichiometric coefficient of 2 PPA2A (A:C):S112/S115 p-SPRY2 PPA2A(A:C):SPRY2