Featured Publications
EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics
Freed DM, Bessman NJ, Kiyatkin A, Salazar-Cavazos E, Byrne PO, Moore JO, Valley CC, Ferguson KM, Leahy DJ, Lidke DS, Lemmon MA. EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics. Cell 2017, 171: 683-695.e18. PMID: 28988771, PMCID: PMC5650921, DOI: 10.1016/j.cell.2017.09.017.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesEpidermal growth factor receptorEGFR ligandsEGFR extracellular regionG protein-coupled receptorsDifferent EGFR ligandsCellular programsDifferent activating ligandsEGFR dimersCell signalingGrowth factor receptorExtracellular regionDimeric conformationEGFR dimerizationNew therapeutic opportunitiesReceptor dimersTyrosine kinaseBreast cancer cellsDimerization strengthActivating ligandsFactor receptorCancer cellsEpigenTherapeutic opportunitiesBiased agonism
2017
Modeling of Receptor Tyrosine Kinase Signaling: Computational and Experimental Protocols
Fey D, Aksamitiene E, Kiyatkin A, Kholodenko BN. Modeling of Receptor Tyrosine Kinase Signaling: Computational and Experimental Protocols. Methods In Molecular Biology 2017, 1636: 417-453. PMID: 28730495, DOI: 10.1007/978-1-4939-7154-1_27.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesReceptor tyrosine kinase signalingMultiple cellular processesTyrosine kinase signalingCellular processesProtein phosphorylationKinase signalingNetwork biologySystems biologyTyrosine kinaseCell survivalIntegration of experimentsPowerful approachIntegrative approachBiologyComputational protocolQuantitative datasetsKinasePhosphorylationSignalingIdentification of salientApoptosisDifferentiationGlucose metabolismRegulation
2003
Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*
Suenaga A, Kiyatkin AB, Hatakeyama M, Futatsugi N, Okimoto N, Hirano Y, Narumi T, Kawai A, Susukita R, Koishi T, Furusawa H, Yasuoka K, Takada N, Ohno Y, Taiji M, Ebisuzaki T, Hoek JB, Konagaya A, Kholodenko BN. Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*. Journal Of Biological Chemistry 2003, 279: 4657-4662. PMID: 14613932, DOI: 10.1074/jbc.m310598200.Peer-Reviewed Original ResearchConceptsPhosphotyrosine bindingTyr-317Shc phosphorylationSH2 domainC-terminal Src homology 2 domainSrc homology 2 domainRas/Raf/MEK/ERK pathwayShc adaptor proteinRaf/MEK/ERK pathwayMEK/ERK pathwayReceptor tyrosine kinasesShc functionPhosphorylated ShcPhosphorylation sitesAdaptor proteinLinker regionShcTyrosine kinaseERK pathwayMembrane receptorsPhosphorylationDomain motionMolecular dynamics simulationsNumerous partnersDomain coupling
2000
Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
Zhang D, Kiyatkin A, Bolin J, Low P. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 2000, 96: 2925-2933. DOI: 10.1182/blood.v96.9.2925.h8002925_2925_2933.Peer-Reviewed Original ResearchCytoplasmic domainP72syk protein tyrosine kinaseGlyceraldehyde-3-phosphate dehydrogenaseProtein-binding domainsGlyceraldehyde-3-phosphateProtein tyrosine kinasesAnimal cell plasma membranesCell plasma membraneCytoplasmic domain of erythrocyte membrane band 3Improved structure definitionBinding domainMultiple proteinsPeripheral proteinsProtein networkPlasma membraneOrganizing centerDimerization armTyrosine kinaseCdb3Protein ligandsBinding sitesConformational changesFunctional interpretationProteinRed blood cell membraneCrystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3
Zhang D, Kiyatkin A, Bolin J, Low P. Crystallographic structure and functional interpretation of the cytoplasmic domain of erythrocyte membrane band 3. Blood 2000, 96: 2925-2933. PMID: 11049968, DOI: 10.1182/blood.v96.9.2925.Peer-Reviewed Original ResearchConceptsCytoplasmic domainPeripheral proteinsAnimal cell plasma membranesRed blood cell membraneProtein tyrosine kinasesGlyceraldehyde-3-phosphate dehydrogenaseErythrocyte membrane band 3Major conformational changesMajor organizing centersCell plasma membraneBand 3Membrane band 3Protein 4.2Dimerization armProtein networkPlasma membraneMultiple proteinsTyrosine kinaseProtein ligandsOrganizing centerConformational changesImproved structural definitionCell membraneProtein 4Protein
1995
Control of erythrocyte metabolism by redox-regulated tyrosine phosphatases and kinases
Low P, Kiyatkin A, Li Q, Harrison M. Control of erythrocyte metabolism by redox-regulated tyrosine phosphatases and kinases. Protoplasma 1995, 184: 196-202. DOI: 10.1007/bf01276920.Peer-Reviewed Original ResearchTyrosine phosphataseN-terminusBand 3Cytoplasmic tyrosine phosphataseGlyceraldehyde-3-phosphate dehydrogenase bindsEnzyme bindingCytoplasmic domainTyrosine phosphorylationTyr-8Tyrosine kinaseElectron transport pathwaysGlycolytic enzymesMetabolic regulationCoordinate mannerTyr-21KinaseNovel mechanismPhosphorylationRedox changesPhosphataseFull activityTransport pathwaysEnzymePathwayBinding