2010
Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells
Bae JH, Boggon TJ, Tomé F, Mandiyan V, Lax I, Schlessinger J. Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 2866-2871. PMID: 20133753, PMCID: PMC2840318, DOI: 10.1073/pnas.0914157107.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesTyrosine autophosphorylationKinase moleculesTyrosine kinaseFGFR1 kinase domainSpecific docking sitesAsymmetric dimer formationFibroblast growth factor receptorActivation of intracellularKinase domainOncogenic activating mutationsGrowth factor receptorMolecular basisDocking siteKinase activityBiochemical experimentsActive enzymeN-lobeC-lobeFGF receptorsFunction mutationsAutophosphorylationTransphosphorylationLiving cellsFactor receptor
2006
Attenuation of signaling pathways stimulated by pathologically activated FGF-receptor 2 mutants prevents craniosynostosis
Eswarakumar VP, Özcan F, Lew ED, Bae JH, Tomé F, Booth CJ, Adams DJ, Lax I, Schlessinger J. Attenuation of signaling pathways stimulated by pathologically activated FGF-receptor 2 mutants prevents craniosynostosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2006, 103: 18603-18608. PMID: 17132737, PMCID: PMC1693709, DOI: 10.1073/pnas.0609157103.Peer-Reviewed Original ResearchConceptsFGF receptorsDocking protein FRS2alphaCommon craniofacial abnormalitySelective uncouplingPremature fusionSkull developmentFunction mutationsDominant mutationsNormal skull developmentMurine model systemMutationsSevere bone disordersModel systemFGFR2cCraniofacial abnormalitiesCalvaria organ culturesPathwayOrgan cultureFRS2alphaSkull vaultMutantsPharmacological approachesFusionFGFRUncoupling