The cell surface receptor FGFRL1 forms constitutive dimers that promote cell adhesion

Rieckmann, Thorsten; Kotevic, Ivana; Trüeb, Beat

doi:10.1016/j.yexcr.2007.10.029

Cited by 41 publications

(70 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This localization pattern is consistent with evidence of FGFRL1 secretory granule association in human embryonic kidney and chondrosarcoma cells (37). We further confirmed that localization to and/or retention at granules is directed by the C-terminal portion of the receptor, with defined truncations showing progressively enhanced localization to the plasma membrane and recycling endosomes (12,31).…”

Section: Discussionsupporting

confidence: 88%

Fibroblast Growth Factor Receptor Like-1 (FGFRL1) Interacts with SHP-1 Phosphatase at Insulin Secretory Granules and Induces Beta-cell ERK1/2 Protein Activation

Silva

Altamentova

Kilkenny

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: FGFRL1 has a unique intracellular domain predicted to inhibit intracellular signaling. Results: FGFRL1 localizes to pancreatic beta-cell insulin granules and enhances intracellular signaling, insulin content, and matrix adhesion. Signaling was reduced by mutation of the intracellular domain. Conclusion: Contrary to prediction, FGFRL1 enhances biological responses in these cells. Significance: This study reveals a novel mechanism of intracellular signaling regulation.

show abstract

Section: Discussionsupporting

confidence: 88%

Fibroblast Growth Factor Receptor Like-1 (FGFRL1) Interacts with SHP-1 Phosphatase at Insulin Secretory Granules and Induces Beta-cell ERK1/2 Protein Activation

Silva

Altamentova

Kilkenny

et al. 2013

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…This possibility is supported by the function of the FGFR-related gene nou-darake in planarian worms, which is similar to Fgfrl1 and inhibits FGF signalling in Xenopus eggs (Cebria et al, 2002). Fluorescence resonance energy transfer (FRET) studies demonstrate that FGFRL1 proteins form constitutive homodimers at the cell surface, which promote cell adhesion properties in a similar way to the nectins (Rieckmann et al, 2008). This is consistent with the phenotypic alterations observed in Fgfrl1 -/-mice, where the absence of Fgfrl1 may adversely affect epithelialto-mesenchymal transition of endocardial cells in the outflow tract cushions or the migration of neural crest cells in the pharyngeal arches.…”

Section: Fgfrl1mentioning

confidence: 99%

Multiple congenital malformations of Wolf-Hirschhorn syndrome are recapitulated inFgfrl1null mice

Catela

Bilbao

Slonimsky

et al. 2009

Disease Models &Amp; Mechanisms

View full text Add to dashboard Cite

SUMMARY Wolf-Hirschhorn syndrome (WHS) is caused by deletions in the short arm of chromosome 4 (4p) and occurs in about one per 20,000 births. Patients with WHS display a set of highly variable characteristics including craniofacial dysgenesis, mental retardation, speech problems, congenital heart defects, short stature and a variety of skeletal anomalies. Analysis of patients with 4p deletions has identified two WHS critical regions (WHSCRs); however, deletions targeting mouse WHSCRs do not recapitulate the classical WHS defects, and the genes contributing to WHS have not been conclusively established. Recently, the human FGFRL1 gene, encoding a putative fibroblast growth factor (FGF) decoy receptor, has been implicated in the craniofacial phenotype of a WHS patient. Here, we report that targeted deletion of the mouse Fgfrl1 gene recapitulates a broad array of WHS phenotypes, including abnormal craniofacial development, axial and appendicular skeletal anomalies, and congenital heart defects. Fgfrl1 null mutants also display a transient foetal anaemia and a fully penetrant diaphragm defect, causing prenatal and perinatal lethality. Together, these data support a wider role for Fgfrl1 in development, implicate FGFRL1 insufficiency in WHS, and provide a novel animal model to dissect the complex aetiology of this human disease.

show abstract

“…In fact, with 26% sequence identity (33% sequence similarity if conservative amino acid substitutions are included), nectin-3 displays, after the classical FGFRs, the best similarity to FGFRL1 of the 42 proteins listed in Table I. Like the nectins, FGFRL1 forms homodimers on the cell membrane as demonstrated by FRET measurements and by immunoprecipitation experiments (11). Furthermore, FGFRL1 occurs preferentially at cell-cell contact sites similar to the nectins.…”

Section: Itim/itam Containing Receptorsmentioning

confidence: 94%

“…Furthermore, recombinant FGFRL1 interacts strongly with heparin and heparan sulfate (9,11). Based on the interaction of the novel receptor with FGF ligands and heparin and on the absence of the tyrosine kinase domain, we speculated that FGFRL1 might function as a decoy receptor that modulates or inhibits FGF signaling (6,9).…”

Section: Introductionmentioning

confidence: 99%

Genome-wide comparison of FGFRL1 with structurally related surface receptors

Zhuang

Falquet²,

Trüeb³

2010

Experimental and Therapeutic Medicine

Self Cite

View full text Add to dashboard Cite

Abstract. FGFRL1 (FGFR5) is a member of the fibroblast growth factor receptor family, which lacks the intracellular tyrosine kinase domain required for signal transduction by trans-phosphorylation. Since it still contains a cytoplasmic domain of 100 amino acid residues with a peculiar histidinerich element, it might be involved in an alternative pathway of downstream signaling. To get a clue about a possible mechanism, we compared the overall structure of FGFRL1 with all proteins from the UniProt databank. We found that the human genome encodes 42 structurally related proteins with a signal peptide, three Ig-like domains and a transmembrane domain. These proteins can be grouped in seven families, fibroblast growth factor receptors (FGFRs), Fc receptor-like proteins, IL-1 receptor-like proteins, killer cell Ig-like receptors (KIRs), nectin-like proteins, sialic acid binding lectins (SIGLECs) and signal regulatory proteins (SIRPs). The 7 families utilize four different strategies for signaling, namely a protein tyrosine kinase domain, a TIR (Toll/IL-1 receptor) domain, ITIM/ ITAM motifs as well as carboxy-terminal peptides that interact with the PDZ domain of an adaptor protein. It remains to be determined whether FGFRL1 might also utilize one of these strategies for signaling.

show abstract

The cell surface receptor FGFRL1 forms constitutive dimers that promote cell adhesion

Cited by 41 publications

References 28 publications

Fibroblast Growth Factor Receptor Like-1 (FGFRL1) Interacts with SHP-1 Phosphatase at Insulin Secretory Granules and Induces Beta-cell ERK1/2 Protein Activation

Fibroblast Growth Factor Receptor Like-1 (FGFRL1) Interacts with SHP-1 Phosphatase at Insulin Secretory Granules and Induces Beta-cell ERK1/2 Protein Activation

Multiple congenital malformations of Wolf-Hirschhorn syndrome are recapitulated inFgfrl1null mice

Genome-wide comparison of FGFRL1 with structurally related surface receptors

Contact Info

Product

Resources

About