PPA2A dephosphorylates SPRY2

Stable Identifier
Reaction [transition]
Homo sapiens
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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.

Literature References
PubMed ID Title Journal Year
17255109 Direct binding of PP2A to Sprouty2 and phosphorylation changes are a prerequisite for ERK inhibition downstream of fibroblast growth factor receptor stimulation

Philp, RJ, Saw, TY, Yusoff, P, Lao, DH, Fong, CW, Chandramouli, S, Jackson, RA, Yu, CY, Guy, GR

J Biol Chem 2007
Catalyst Activity

protein serine/threonine phosphatase activity of PPA2A (A:C):S112/S115 p-SPRY2 [cytosol]

Orthologous Events
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