Activated FGFR1 binds FLRT1,2,3

Stable Identifier
Reaction [binding]
Homo sapiens
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The three fibronectin-leucine-rich transmembrane (FLRT) proteins were identified as positive regulators of FGFR signaling that enhance FGFR-dependent RAS/MAPK pathway activation. All three FLRT proteins have been shown to interact with FGFR1 by co-immunoprecipitation and, at least in the case of FLRT3, the interaction is mediated by the FLRT fibronectin-like domain (Bottcher et al, 2004; Haines et al, 2006). Each FLRT gene has a distinct expression pattern and the strength of the protein-protein interaction with the FGF receptor varies, allowing for cell-type specific modulation of signaling activity (Haines et al, 2006). How the FLRT proteins act to enhance FGFR-dependent MAPK pathway activation is not clear, however FLRT1 has recently been shown to be phosphorylated in an FGFR1- and Src family kinase (SFK)-dependent manner (Wheldon et al, 2010).

Literature References
PubMed ID Title Journal Year
16872596 Regulated expression of FLRT genes implies a functional role in the regulation of FGF signalling during mouse development

Rigby, PW, Summerbell, D, Heath, JK, Haines, BP, Wheldon, LM

Dev. Biol. 2006
20421966 Critical role of FLRT1 phosphorylation in the interdependent regulation of FLRT1 function and FGF receptor signalling

Mason, I, Heath, JK, Haines, BP, Rajappa, R, Wheldon, LM, Rigby, PW

PLoS ONE 2010
14688794 The transmembrane protein XFLRT3 forms a complex with FGF receptors and promotes FGF signalling

Niehrs, C, Böttcher, RT, Delius, H, Pollet, N

Nat. Cell Biol. 2004
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