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Fgfrl1b is required for proper formation of all ventral cartilage elements and acts cooperatively with Fgfrl1a during gill cartilage formation.
FGFRL1 contains three extracellular Ig-like domains and a single transmembrane domain. It lacks the intracellular tyrosine kinase domain, but contains a short intracellular tail with a peculiar histidine-rich motif.The reason why this motif was conserved during evolution in most species, but not in mice, is not clear.
FgfrL1 is specifically required for embryonic development of slow muscle fibers.
Evidence that the novel receptor FGFRL1 signals indirectly via FGFR1.
FGFRL1 does not function as a decoy receptor in beta-cells, but rather it enhances ERK1/2 signaling through association of SHP-1 with the receptor's intracellular SH2-binding motif.
The expression profiles of wildtype and Fgfrl1 mutant kidneys, were compared to identify genes that act downstream of Fgfrl1 signaling during the early steps of nephron formation.
Fgfrl1 null mice have reduced expression of Tpm3, sarcomere genes and Lrtm1 in the diaphragm.
FGFRL1 is indeed a decoy receptor for FGFs.
FGFRL1 expression is very low in mouse embryos of day 6 but steadily increases until birth.
Mice with a targeted disruption of the Fgfrl1 gene die at birth due to alterations in the diaphragm.
These data support a wider role for Fgfrl1 in development, implicate FGFRL1 insufficiency in Wolf-Hirschhorn syndrome, and provide a novel animal model to dissect the complex aetiology of this human disease.
this study shows FGFRL1 promotes ovarian cancer progression by crosstalk with Hedgehog signaling
FGFRL1 is a transmembrane receptor that can induce the fusion of CHO cells to multinucleated syncytia. This cell fusion activity has been attributed to the extracellular Ig3 domain of the receptor. The Ig3 domain from humans, mice, chicken and fish stimulates fusion of CHO cells, while the Ig3 domain from lancelet and sea urchin does not.
Both in vitro and in vivo studies determined that miR-210 promoted hepatocellular carcinoma (HCC), angiogenesis, and the corresponding mechanism was identified to be the direct targeting and inhibition of fibroblast growth factor receptor-like 1 (FGFRL1) expression
FGFRL1 is a cell adhesion protein.
functional evidence for a novel FGFRL1 poly-miRTS rs4647940 in a previously known 4p16.3 locus, and experimental and clinical genetics studies have shown both FGFRL1 and hsa-miR-140-5p are important for bone formation.
Cell-cell fusion induced by the Ig3 domain of receptor FGFRL1
The signaling complex appears to integrate the input from FGFR and EphA4, and release the output signal through FRS2alpha.
study identified a novel region of deletion mapping to 4p16.3 in 15 percent of bladder tumors and 24 percent of bladder cancer cell lines; FGFRL1, which maps within this region, was investigated as putative deletion target; average FGFRL1 protein expression was lower in bladder tumors compared to normal tissue, but downregulation was independent from 4p16.3 LOH status
Interaction of FGFRL1 with Spred1 increases the proportion of the receptor at the plasma membrane.
an important role for miR-210 as a tumor-suppressive microRNA with effects on cancer cell proliferation
FGFRL1 is capable of inducing syncytium formation of heterologous cells in vitro.
analysis of FGF18 and FGFR5(FGFRL1) expression in primary endothelial cells and vascular smooth muscle cells
Screening of 241 different human tumors with the help of a cancer profiling array suggested major alterations in the relative expression of FGFRL1 in ovarian tumors
The extracellular domain of recombinant FGFRL1 promoted cell adhesion, but not cell spreading. Adhesion was mediated by heparan sulfate glycosaminoglycans located at the cell surface.
mutant FGFRL1 contributes to the skeletal malformations of the patient
Xenopus FGF receptor-like 1/nou-darake expression patterns in early Xenopus development resemble those of planarian nou-darake and Xenopus FGF8
The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A marked difference between this gene product and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found for this gene.
, fibroblast growth factor receptor-like 1
, FGF receptor-like protein 1
, fibroblast growth factor receptor 5
, fibroblast growth factor receptor-like protein
, FGF homologous factor receptor
, FGFR-like protein
, FGF receptor-like protein
, Fibroblast growth factor receptor-like 1
, fibroblast growth factor receptor like 1
, FGF receptor-like protein 1b beta
, fibroblast growth factor receptor-like 1b