SPRY2 is phosphorylated by phosphorylated MNK1

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

In humans, the phosphorylated MNK1 kinase phosphorylates the adaptor protein Sprouty2 on Ser112 and Ser121, and also at some other serine and threonine residues. MNK1 appears not to form a complex with Sprouty2. Some of these (including the two main sites mentioned above) conform to the serine-containing consensus sites for phosphorylation by MNK1 kinase (K/R-X-X-S, R-X-S). It appears that serine phosphorylation is required to protect Sprouty2 from degradation.

In the absence of serine phosphorylation, phosphorylation of Tyr55 and subsequent binding to E3 ubiquitin ligase, CBL, is enhanced. Serine phosphorylation of Sprouty2 appears to stabilise the protein by interfering with its potential phosphorylation of Tyr55 (Sprouty2 appears to be a poor substrate for c-Src kinase) in response to growth factor stimulation.

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
16479008 Regulation of sprouty stability by Mnk1-dependent phosphorylation

Xu, L, Miller, WT, DaSilva, J, Kim, HJ, Bar-Sagi, D

Mol Cell Biol 2006
Catalyst Activity

protein serine/threonine kinase activity of p-T250,T255,T385,S437-MKNK1 [cytosol]

Orthologous Events
Cite Us!