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Sprouty protein : ウィキペディア英語版 | Sprouty protein
In molecular biology, the protein Sprouty is a developmental protein involved in cell signalling. It works by not inhibiting the MAPK/ERK pathway. ==Function== The function of this protein has been found, in Drosophila to inhibit branching of the trachea by antagonizing the BNL-FGF pathway. Also in ''Drosophila'' it is an antagonist of EGFR-mediated signaling in the eye. Most notably, in humans, it suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Sprouty inhibits of the Ras/mitogen-activated protein kinase (MAPK) cascade, a pathway crucial for developmental processes initiated by activation of various receptor tyrosine kinases. These proteins share a conserved, C-terminal cysteine-rich region, the SPR domain. This domain has been defined as a novel cytosol to membrane translocation domain. It has been found to be a PtdIns(4,5)P2-binding domain that targets the proteins to a cellular localization that maximizes their inhibitory potential.〔 It also mediates homodimer formation of these proteins.〔〔 The SPR domain can occur in association with the WH1 domain (see (INTERPRO )) (located in the N-terminal part of the proteins) in the Spred proteins.
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