ArticleThe Journal of biological chemistry2011
FGFR3 heterodimerization in achondroplasia, the most common form of human dwarfism.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Spatiotemporal Regulation and Lineage Specification in Embryonic Endochondral Ossification.International journal of molecular sciences · 2026Review
- Measurement of FGFR3 signaling at the cell membrane via total internal reflection fluorescence microscopy to compare the activation of FGFR3 mutants.The Journal of biological chemistry · 2023Article
- Determining the statistical significance of the difference between arbitrary curves: A spreadsheet method.PloS one · 2023Article
- Inhibition of Streptococcus mutans biofilms with bacterial-derived outer membrane vesicles.BMC microbiology · 2021Article
- High-resolution computed tomography temporal bone imaging in achondroplasia.Proceedings (Baylor University. Medical Center) · 2021Article
- The transition model of RTK activation: A quantitative framework for understanding RTK signaling and RTK modulator activity.Cytokine & growth factor reviews · 2019Review
- Skeletal Characterization of the Fgfr3 Mouse Model of Achondroplasia Using Micro-CT and MRI Volumetric Imaging.Scientific reports · 2018Article
- Quantifying the Interaction between EGFR Dimers and Grb2 in Live Cells.Biophysical journal · 2017Article
- Achondroplasia: Development, pathogenesis, and therapy.Developmental dynamics : an official publication of the American Association of Anatomists · 2017Review
- A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors.The Journal of biological chemistry · 2017Article
- Pathogenic Cysteine Removal Mutations in FGFR Extracellular Domains Stabilize Receptor Dimers and Perturb the TM Dimer Structure.Journal of molecular biology · 2016Article
- Effect of the achondroplasia mutation on FGFR3 dimerization and FGFR3 structural response to fgf1 and fgf2: A quantitative FRET study in osmotically derived plasma membrane vesicles.Biochimica et biophysica acta · 2016Article
- Bilateral ossiculoplasty in 1 case of achondroplasia.Korean journal of audiology · 2013Article
- FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.Biophysical journal · 2013Article
- Multiple consequences of a single amino acid pathogenic RTK mutation: the A391E mutation in FGFR3.PloS one · 2013Article
- Physical-chemical principles underlying RTK activation, and their implications for human disease.Biochimica et biophysica acta · 2012Review
- Transmembrane helix dimerization: beyond the search for sequence motifs.Biochimica et biophysica acta · 2012Review
- Consequences of replacing EGFR juxtamembrane domain with an unstructured sequence.Scientific reports · 2012Article
- Direct assessment of the effect of the Gly380Arg achondroplasia mutation on FGFR3 dimerization using quantitative imaging FRET.PloS one · 2012Article
- Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The G380R mutation in the transmembrane domain of fibroblast growth factor receptor 3 (FGFR3) causes achondroplasia, the most common form of human dwarfism. Achondroplasia is a heterozygous disorder, and thus the affected individuals express both wild-type and mutant FGFR3. Yet heterodimerization in achondroplasia has not been characterized thus far. To investigate the formation of FGFR3 heterodimers in cellular membranes, we designed an FGFR3 construct that lacks the kinase domain, and we monitored the formation of inactive heterodimers between this construct and wild-type and mutant FGFR3. The formation of the inactive heterodimers depleted the pool of full-length receptors capable of forming active homodimers and ultimately reduced their phosphorylation. By analyzing the effect of the truncated FGFR3 on full-length receptor phosphorylation, we demonstrated that FGFR3 WT/G380R heterodimers form with lower probability than wild-type FGFR3 homodimers at low ligand concentration. These results further our knowledge of FGFR3-associated bone disorders.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.