2023
Heparin is essential for optimal cell signaling by FGF21 and for regulation of βKlotho cellular stability
An S, Mohanty J, Tome F, Suzuki Y, Lax I, Schlessinger J. Heparin is essential for optimal cell signaling by FGF21 and for regulation of βKlotho cellular stability. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2219128120. PMID: 36745784, PMCID: PMC9962926, DOI: 10.1073/pnas.2219128120.Peer-Reviewed Original ResearchConceptsHeparan sulfate proteoglycanCellular stabilityCell membraneSingle-molecule fluorescenceProtein kinase responsesChinese hamster ovary cellsFGF moleculesHamster ovary cellsFactor bindsReceptor assemblyReceptor dimerizationGrowth factor bindsHigh-affinity bindingFGF1 stimulationKinase responseCHO cellsOvary cellsSulfate proteoglycanIntracellular CaKlotho proteinFGFR1cPotential roleRegulationΒKlothoCells
2015
Augmentor α and β (FAM150) are ligands of the receptor tyrosine kinases ALK and LTK: Hierarchy and specificity of ligand–receptor interactions
Reshetnyak AV, Murray PB, Shi X, Mo ES, Mohanty J, Tome F, Bai H, Gunel M, Lax I, Schlessinger J. Augmentor α and β (FAM150) are ligands of the receptor tyrosine kinases ALK and LTK: Hierarchy and specificity of ligand–receptor interactions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 15862-15867. PMID: 26630010, PMCID: PMC4702955, DOI: 10.1073/pnas.1520099112.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnaplastic Lymphoma KinaseAnimalsCell LineCell Line, TumorCell ProliferationCytokinesDoxycyclineEnzyme ActivationHEK293 CellsHeparinHumansImmunoblottingLigandsMiceMolecular Sequence DataNIH 3T3 CellsProtein BindingReceptor Protein-Tyrosine KinasesSequence Homology, Amino AcidConceptsLeukocyte tyrosine kinaseReceptor tyrosine kinasesTyrosine kinaseIL-3-independent growthCritical cellular functionsBa/F3 cellsCell surface receptorsAnaplastic lymphoma kinaseLigand-receptor interactionsCellular functionsLigand bindingF3 cellsReceptor tyrosineProtein ligandsNIH/3T3 cellsKinaseSurface receptorsIndependent growthSubnanomolar potencyCellsDisease statesHigh affinityLymphoma kinaseFAM150ANovel cytokine
2014
The Strength and Cooperativity of KIT Ectodomain Contacts Determine Normal Ligand-Dependent Stimulation or Oncogenic Activation in Cancer
Reshetnyak AV, Opatowsky Y, Boggon TJ, Folta-Stogniew E, Tome F, Lax I, Schlessinger J. The Strength and Cooperativity of KIT Ectodomain Contacts Determine Normal Ligand-Dependent Stimulation or Oncogenic Activation in Cancer. Molecular Cell 2014, 57: 191-201. PMID: 25544564, PMCID: PMC4764128, DOI: 10.1016/j.molcel.2014.11.021.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviridaeBinding SitesCrystallography, X-RayEnzyme ActivationHumansLigandsMiceModels, MolecularMutationNeoplasmsNIH 3T3 CellsProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, SecondaryProto-Oncogene Proteins c-kitRecombinant ProteinsSf9 CellsSpodopteraConceptsOncogenic KIT mutationsKIT mutationsGastrointestinal stromal tumorsAcute myeloid leukemiaKIT tyrosine kinase activitySomatic oncogenic mutationsInterstitial pacemaker cellsLigand-dependent stimulationReceptor tyrosine kinase KITStromal tumorsTyrosine kinase KITMyeloid leukemiaReceptor activationPacemaker cellsTyrosine kinase activityCancerKinase KITOncogenic mutationsHematopoietic cellsGerm cellsOncogenic activationActivationCellsReceptor moleculesMutations