| First Author | Cabrita MA | Year | 2006 |
| Journal | J Biol Chem | Volume | 281 |
| Issue | 39 | Pages | 29201-12 |
| PubMed ID | 16877379 | Mgi Jnum | J:116930 |
| Mgi Id | MGI:3695236 | Doi | 10.1074/jbc.M603921200 |
| Citation | Cabrita MA, et al. (2006) A functional interaction between sprouty proteins and caveolin-1. J Biol Chem 281(39):29201-2912 |
| abstractText | Growth factor-mediated signal transduction cascades can be regulated spatio-temporally by signaling modulators, such as Sprouty proteins. The four mammalian Sprouty family members are palmitoylated phosphoproteins that can attenuate or potentiate numerous growth factor-induced signaling pathways. Previously, we have shown that Sprouty-1 and Sprouty-2 associate with Caveolin-1, the major structural protein of caveolae. Like Sprouty, Caveolin-1 inhibits growth factor-induced mitogen-activated protein kinase activation. Here, we demonstrate that all four mammalian Sprouty family members physically interact with Caveolin-1. The C terminus of Caveolin-1 is the major Sprouty-binding site, whereas Sprouty binds Caveolin-1 via its conserved C-terminal domain. A single point mutation in this domain results in loss of Caveolin-1 interaction. Moreover, we demonstrate that the various Sprouty isoforms differ dramatically in their cooperation with Caveolin-1-mediated inhibition of mitogen-activated protein kinase activation and that such cooperation is also highly dependent on the type of growth factor investigated and on cell density. Together, the data suggest that the Sprouty/Caveolin-1 interaction modulates signaling in a growth factor- and Sprouty isoform-specific manner. |
