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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 (show Slc25a1 Proteins) urchin does not.
Both in vitro and in vivo studies determined that miR (show MLXIP Proteins)-210 promoted hepatocellular carcinoma (HCC (show FAM126A Proteins)), 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 (show CD24 Proteins)-miR (show MLXIP Proteins)-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 (show FGFR2 Proteins) and EphA4 (show EPHA4 Proteins), and release the output signal through FRS2alpha (show FRS2 Proteins).
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 (show SPRED1 Proteins) increases the proportion of the receptor at the plasma membrane.
an important role for miR (show MLXIP Proteins)-210 as a tumor-suppressive microRNA with effects on cancer cell proliferation
FGFRL1 is capable of inducing syncytium formation of heterologous cells in vitro.
FGFRL1 contains three extracellular Ig-like domains and a single transmembrane domain. It lacks the intracellular tyrosine kinase (show TYRO3 Proteins) 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 (show FGFR1 Proteins).
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.
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.
FGF homologous factor receptor
, FGF receptor-like protein 1
, FGFR-like protein
, fibroblast growth factor receptor 5
, fibroblast growth factor receptor-like protein