SPRY2 is serine phosphorylated in response to MAPK activation

Stable Identifier
Reaction [omitted]
Homo sapiens
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Some evidence suggests that SPRY2 can exert its negative role on FGF signaling at the level of RAF activation. Hypophosphorylated SPRY2 binds to inactive B-RAF, preventing it from activating ERK signaling. MAPK activation results in phosphorylation of SPRY2 on six serine residues (S7, S42, S111, S120, S140 and S167), and inhibits B-RAF binding. Phosphorylation of serine residues 111 and 120 on SPRY2 requires MAPK activation, however the identity of the phosphorylating kinase has not been established. Phosphorylation at these two site (S111 and S120) directly affects B-RAF binding while the remaining four sites appear to contribute indirectly. Oncogenic forms of B-RAF such as B-RAF V600E, which adopt active kinase conformations, do not associate with SPRY2, regardless of its phosphorylation status. This suggests that two mechanisms affect the SPRY2:B-RAF interaction: SPRY2 phosphorylation and B-RAF conformation.
Literature References
PubMed ID Title Journal Year
19690147 Sprouty2 association with B-Raf is regulated by phosphorylation and kinase conformation

Brady, SC, Coleman, ML, Olson, MF, Feller, SM, Munro, J, Morrice, NA

Cancer Res 2009
11698404 Sprouty2 inhibits the Ras/MAP kinase pathway by inhibiting the activation of Raf

Lo, TL, Lao, DH, Yusoff, P, Fong, CW, Ong, SH, Wong, ES, Lim, J, Leong, HF, Guy, GR

J Biol Chem 2002
This event is regulated
Orthologous Events
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