2020
FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho
Suzuki Y, Kuzina E, An SJ, Tome F, Mohanty J, Li W, Lee S, Liu Y, Lax I, Schlessinger J. FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 31800-31807. PMID: 33257569, PMCID: PMC7749347, DOI: 10.1073/pnas.2018554117.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCalcinosisCell MembraneFibroblast Growth Factor-23Fibroblast Growth FactorsGlucuronidaseHEK293 CellsHumansHyperostosis, Cortical, CongenitalHyperphosphatemiaImmunoglobulin Fc FragmentsKlotho ProteinsMutationOsteomalaciaProtein BindingProtein DomainsProtein MultimerizationRecombinant Fusion ProteinsRickets, HypophosphatemicConceptsFGF receptorsTotal internal reflection fluorescence microscopyChimeric receptor moleculesReflection fluorescence microscopyBinding sitesDisulfide bridge formationCritical metabolic processesMAPK responseCytoplasmic domainGrowth factor familyTerminal tailFactor familyKinase activationSimilar binding affinitiesExtracellular domainFGFR1 activationTandem repeatsMetabolic processesDisulfide bridgesCell surfaceDistinct ligandsCell membraneFluorescence microscopyDistinct high-affinity binding sitesPhosphate homeostasis
2018
Identification of a biologically active fragment of ALK and LTK-Ligand 2 (augmentor-α)
Reshetnyak AV, Mohanty J, Tomé F, Puleo DE, Plotnikov AN, Ahmed M, Kaur N, Poliakov A, Cinnaiyan AM, Lax I, Schlessinger J. Identification of a biologically active fragment of ALK and LTK-Ligand 2 (augmentor-α). Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 8340-8345. PMID: 30061385, PMCID: PMC6099872, DOI: 10.1073/pnas.1807881115.Peer-Reviewed Original ResearchConceptsLeukocyte tyrosine kinaseN-terminal variable regionDeletion mutantsVariable regionsDisulfide bridgesDetailed biochemical characterizationIntramolecular disulfide bridgesNIH 3T3 cellsSimilar tyrosine phosphorylationAnaplastic lymphoma kinaseReceptor-receptor interactionsMAP kinase responseTyrosine phosphorylationBiochemical characterizationTyrosine kinaseReceptor tyrosineNeuronal differentiationL6 cellsPhysiological roleMode of actionKinase responseCultured cellsPC12 cells