SRC phosphorylates SPRY2 on Y55 and Y227

Stable Identifier
Reaction [transition]
Homo sapiens
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Sprouty 2 protein is phosphorylated on tyrosine residue 55. The ability of SRC kinase to catalyze this reaction has been demonstrated with purified proteins in vitro (Li et al. 2004) and in cultured cells with studies of the effects of SRC-family pharmacological inhibitors and of dominant-negative mutant SRC proteins (Mason et al. 2004). SRC kinase also phosphorylates numerous tyrosine residues in the C terminal region of SPRY2 including Y227, in response to FGF but not EGF stimulation. SRC-mediated phosphorylation of SPRY2 at Y55 is negatively regulated by MNK1-dependent serine phosphorylation of SPRY2. MNK1-mediated SPRY2 phosphorylation stabilizes SPRY2 by antagonizing tyrosine phosphorylation and CBL binding, thus limiting ubiquitin-mediated degradation.

Literature References
PubMed ID Title Journal Year
15637081 Phosphorylation of carboxyl-terminal tyrosines modulates the specificity of Sprouty-2 inhibition of different signaling pathways

Yarden, Y, Ron, D, Vaisman, N, Zwang, Y, Rubin, C

J Biol Chem 2005
15004239 Tyrosine phosphorylation of Sprouty proteins regulates their ability to inhibit growth factor signaling: a dual feedback loop

Gross, I, Mason, JM, Dimri, M, Licht, JD, Band, H, Morrison, DJ, Bassit, B

Mol Biol Cell 2004
15564375 FRS2-dependent SRC activation is required for fibroblast growth factor receptor-induced phosphorylation of Sprouty and suppression of ERK activity

Brunton, VG, Burgar, HR, Heath, JK, Li, X, Wheldon, LM

J Cell Sci 2004
Catalyst Activity

protein tyrosine kinase activity of SRC-1 [plasma membrane]

This event is regulated