loading...| Preferred Name | SPRY2 is serine phosphorylated in response to MAPK activation | |
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Reviewed: Gotoh, N, 2011-08-26 Authored: Rothfels, K, 2011-08-15 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 at 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. |
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http://purl.obolibrary.org/obo/HINO_0009056 |
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Reviewed: Gotoh, N, 2011-08-26 Authored: Rothfels, K, 2011-08-15 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 at 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. |
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Reactome, http://www.reactome.org Pubmed11698404 Pubmed19690147 |
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SPRY2 is serine phosphorylated in response to MAPK activation |
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HINO:0009056 |
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SPRY2 is serine phosphorylated in response to MAPK activation |
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Reactome Database ID Release 431295634 ReactomeREACT_111121 |
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