Sprouty protein

In molecular biology, the protein Sprouty is a developmental protein involved in cell signalling. It works by inhibiting the MAPK/ERK pathway.

Sprouty
Identifiers
Symbol	Sprouty
Pfam	PF05210
InterPro	IPR007875
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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.^[1][2][3][4] 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.^[2][5] It also mediates homodimer formation of these proteins.^[1][5]

The SPR domain can occur in association with the WH1 domain (see INTERPRO) (located in the N-terminal part of the proteins) in the Spread proteins.