ArticleProtein science : a publication of the Protein Society2009
The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control.Cells · 2025Review
- Fibroblast Growth Factor Receptors (FGFRs) and Noncanonical Partners in Cancer Signaling.Cells · 2021Review
- The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins.The Journal of membrane biology · 2019Review
- Review
- Targeting Tyrosine kinases in Renal Cell Carcinoma: "New Bullets against Old Guys".International journal of molecular sciences · 2019Review
- Targeting Cellular Trafficking of Fibroblast Growth Factor Receptors as a Strategy for Selective Cancer Treatment.Journal of clinical medicine · 2018Review
- Primary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations.Biochemistry · 2014Article
- Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies.Structure (London, England : 1993) · 2013Article
- Extracellular assembly and activation principles of oncogenic class III receptor tyrosine kinases.Nature reviews. Cancer · 2012Review
- Self-association of models of transmembrane domains of ErbB receptors in a lipid bilayer.Biophysical journal · 2010Article
- Left-handed dimer of EphA2 transmembrane domain: Helix packing diversity among receptor tyrosine kinases.Biophysical journal · 2010Article
- Article
- Understanding cytokine and growth factor receptor activation mechanisms.Critical reviews in biochemistry and molecular biologyReview
- Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?Cell adhesion & migrationReview
- Structure elucidation of dimeric transmembrane domains of bitopic proteins.Cell adhesion & migrationReview
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3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The fibroblast growth factor receptor 3 (FGFR3) is a member of the FGFR subfamily of the receptor tyrosine kinases (RTKs) involved in signaling across the plasma membrane. Generally, ligand binding leads to receptor dimerization and activation. Dimerization involves the transmembrane (TM) domain, where mutations can lead to constitutive activation in certain cancer types and also in skeletal malformations. Thus, it has been postulated that FGFR homodimerization must be inherently weak to allow regulation, a feature reminiscent of alpha and beta integrin TM interactions. However, we show herein that in FGFR3-TM, four C-terminal residues, CRLR, have a profound destabilizing effect in an otherwise strongly dimerizing TM peptide. In the absence of these four residues, the dimerizing propensity of FGFR3-TM is comparable to glycophorin, as shown using various detergents. In addition, the expected enhanced dimerization induced by the mutation associated to the Crouzon syndrome A391E, was observed only when these four C-terminal residues were present. In the absence of these four residues, A391E was dimer-destabilizing. Finally, using site specific infrared dichroism and convergence with evolutionary conservation data, we have determined the backbone model of the FGFR3-TM homodimer in model lipid bilayers. This model is consistent with, and correlates with the effects of, most known pathological mutations found in FGFR-TM.
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