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doi: 10.1242/10.1242/jcs.00652
Commentary |
Signal Transduction Laboratory, Institute of Molecular and Cell Biology, 30 Medical Drive, Singapore 117 609, Republic of Singapore
* Author for correspondence (e-mail: mcbgg{at}imcb.nus.edu.sg)
Since the discovery of the prototypical Sprouty (Spry) protein in
Drosophila, there has been an effort to determine how these novel
modulators of the Ras/MAP-kinase pathway function. A clue to their mechanism
of action comes from the several highly conserved sequences within all the
currently known Spry isoforms: an 
110-residue cysteine-rich sequence in
the C-terminal half that directs Spry proteins to a concentration of signaling
proteins at the plasma membrane; a small motif surrounding a tyrosine residue
(Y55 in human Spry2) that is responsible for interaction with other proteins.
In cultured mammalian cells, hSpry2 inhibits epidermal growth factor receptor
(EGFR) endocytosis and subsequently sustains the activation of MAP kinase but
negatively regulates the same pathway following stimulation of fibroblast
growth factor receptors (FGFRs). Current evidence indicates that Cbl is a key
protein that interacts directly with Spry2 following activation of receptor
tyrosine kinases (RTKs). It appears to be the ability of Cbl to interact as an
E3 ubiquitin ligase on specific target proteins and as a docking protein in
other contexts that dictates the differential effects Spry2 has on the
Ras/MAP-kinase pathway following EGFR and FGFR activation.
Key words: Sprouty, Fibroblast growth factor, Receptor tyrosine kinase, Epidermal growth factor receptor, MAP kinase
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