2015
Structural analysis of the mechanism of phosphorylation of a critical autoregulatory tyrosine residue in FGFR1 kinase domain
Kobashigawa Y, Amano S, Yokogawa M, Kumeta H, Morioka H, Inouye M, Schlessinger J, Inagaki F. Structural analysis of the mechanism of phosphorylation of a critical autoregulatory tyrosine residue in FGFR1 kinase domain. Genes To Cells 2015, 20: 860-870. PMID: 26300540, DOI: 10.1111/gtc.12277.Peer-Reviewed Original ResearchConceptsFGFR1 kinase domainKinase domainFibroblast growth factor receptor 1Catalytic domainCovalent cross-linking experimentsReceptor tyrosine kinase activationNormal cellular processesSignal transduction pathwaysNonreceptor tyrosine kinaseMechanism of phosphorylationTyrosine kinase activationCross-linking experimentsInitial phosphorylation stepActivation loopCellular processesTransient dimer formationTransduction pathwaysTyrosine phosphorylationGrowth factor receptor 1Domain interactionsKinase activationMutational analysisContact sitesMolecular mechanismsTyrosine residues
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