ArticleBiophysical journal2013
FGFR3 transmembrane domain interactions persist in the presence of its extracellular domain.
Article in Biophysical journal, 2013. 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.
- Article
- Piecing it together: Unraveling the elusive structure-function relationship in single-pass membrane receptors.Biochimica et biophysica acta. Biomembranes · 2017Review
- A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors.The Journal of biological chemistry · 2017Article
- Free Energy Landscape of Lipid Interactions with Regulatory Binding Sites on the Transmembrane Domain of the EGF Receptor.The journal of physical chemistry. B · 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
- Unliganded EphA3 dimerization promoted by the SAM domain.The Biochemical journal · 2015Article
- Activation of transmembrane cell-surface receptors via a common mechanism? The "rotation model".BioEssays : news and reviews in molecular, cellular and developmental biology · 2015Review
- Characterization of membrane protein interactions in plasma membrane derived vesicles with quantitative imaging Förster resonance energy transfer.Accounts of chemical research · 2015Article
- Analytical characterization of plasma membrane-derived vesicles produced via osmotic and chemical vesiculation.Biochimica et biophysica acta · 2015Article
- FGFR3 unliganded dimer stabilization by the juxtamembrane domain.Journal of molecular biology · 2015Article
- Effect of thanatophoric dysplasia type I mutations on FGFR3 dimerization.Biophysical journal · 2015Article
- Dimerization of the EphA1 receptor tyrosine kinase transmembrane domain: Insights into the mechanism of receptor activation.Biochemistry · 2014Article
- Strong dimerization of wild-type ErbB2/Neu transmembrane domain and the oncogenic Val664Glu mutant in mammalian plasma membranes.Biochimica et biophysica acta · 2014Article
- The FRET signatures of noninteracting proteins in membranes: simulations and experiments.Biophysical journal · 2014Article
- Primary and secondary dimer interfaces of the fibroblast growth factor receptor 3 transmembrane domain: characterization via multiscale molecular dynamics simulations.Biochemistry · 2014Article
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Authors and funding
2 authors.
Funding
Abstract
Isolated receptor tyrosine kinase transmembrane (TM) domains have been shown to form sequence-specific dimers in membranes. Yet, it is not clear whether studies of isolated TM domains yield knowledge that is relevant to full-length receptors or whether the large glycosylated extracellular domains alter the interactions between the TM helices. Here, we address this question by quantifying the effect of the pathogenic A391E TM domain mutation on the stability of the fibroblast growth factor receptor 3 dimer in the presence of the extracellular domain and comparing these results to the case of the isolated TM fibroblast growth factor receptor 3 domains. We perform the measurements in plasma membrane-derived vesicles using a Förster-resonance-energy-transfer-based method. The effect of the mutation on dimer stability in both cases is the same (∼-1.5 kcal/mol), suggesting that the interactions observed in simple TM-peptide model systems are relevant in a biological context.
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Registered trials
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