2024
De novo-designed transmembrane proteins bind and regulate a cytokine receptor
Mravic M, He L, Kratochvil H, Hu H, Nick S, Bai W, Edwards A, Jo H, Wu Y, DiMaio D, DeGrado W. De novo-designed transmembrane proteins bind and regulate a cytokine receptor. Nature Chemical Biology 2024, 20: 751-760. PMID: 38480980, PMCID: PMC11142920, DOI: 10.1038/s41589-024-01562-z.Peer-Reviewed Original ResearchTM proteinsTM regionTarget membrane proteinsComplex biological functionsTM domainTM helicesInteraction partnersTransmembrane proteinsMembrane proteinsReceptor homodimerizationBiological functionsCytokine receptorsBinding topologyAmino acidsProteinErythropoietin receptorHomodimerizationCell proliferationTransmembraneEpoRIn vitroMolecular modelingBinding modeReceptorsMotif
2021
EpoR stimulates rapid cycling and larger red cells during mouse and human erythropoiesis
Hidalgo D, Bejder J, Pop R, Gellatly K, Hwang Y, Maxwell Scalf S, Eastman AE, Chen JJ, Zhu LJ, Heuberger JAAC, Guo S, Koury MJ, Nordsborg NB, Socolovsky M. EpoR stimulates rapid cycling and larger red cells during mouse and human erythropoiesis. Nature Communications 2021, 12: 7334. PMID: 34921133, PMCID: PMC8683474, DOI: 10.1038/s41467-021-27562-4.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnimalsAntigens, CDbcl-X ProteinCD4 AntigensCell CycleCell DifferentiationCell NucleusCell SizeCell SurvivalCyclin-Dependent Kinase Inhibitor p27Embryo, MammalianErythroblastsErythrocytesErythropoiesisErythropoietinFemaleFetusHealthy VolunteersHumansIronLiverMaleMice, Inbred C57BLModels, BiologicalProtein Serine-Threonine KinasesReceptors, ErythropoietinReceptors, TransferrinReticulocytesSignal TransductionConceptsCell size regulationCell sizeSequential cell divisionsEpoR functionErythroblast survivalMouse erythroblastsCell divisionSize regulationHuman erythropoiesisErythropoietin receptorCell cycleEpoRHypoxic stressRed cell sizeHigh erythropoietinLarger red cellsWild-type miceCyclingErythroblastsRegulationHigher EPO levelsMiceRed cellsSurvivalErythropoiesis
2019
Transmembrane Protein Aptamer Induces Cooperative Signaling by the EPO Receptor and the Cytokine Receptor β-Common Subunit
He L, Cohen EB, Edwards APB, Xavier-Ferrucio J, Bugge K, Federman RS, Absher D, Myers RM, Kragelund BB, Krause DS, DiMaio D. Transmembrane Protein Aptamer Induces Cooperative Signaling by the EPO Receptor and the Cytokine Receptor β-Common Subunit. IScience 2019, 17: 167-181. PMID: 31279934, PMCID: PMC6614117, DOI: 10.1016/j.isci.2019.06.027.Peer-Reviewed Original ResearchErythropoietin receptorPrimary human hematopoietic progenitor cellsProtein aptamerGrowth factor independenceHuman hematopoietic progenitor cellsJAK/STATMurine BaF3 cellsTransmembrane domainCellular processesCytoplasmic tyrosinesCytoplasmic domainHematopoietic progenitor cellsErythroid differentiationBaF3 cellsCommon subunitFactor independenceSerum withdrawalCell deathCooperative signalingEPO receptorEPOR homodimersProgenitor cellsEssential roleSubunitsSignaling
2017
Bone marrow endothelial cells induce immature and mature B cell egress in response to erythropoietin
Ito T, Hamazaki Y, Takaori-Kondo A, Minato N. Bone marrow endothelial cells induce immature and mature B cell egress in response to erythropoietin. Cell Structure And Function 2017, 42: 17018. PMID: 29070774, DOI: 10.1247/csf.17018.Peer-Reviewed Original ResearchConceptsBone marrow endothelial cellsMarrow endothelial cellsStromal cellsEndothelial cellsEmergency hematopoiesisBone marrow stromal cellsMature B cellsPhosphorylation of STAT5Immature B cellsSpecific lineagesB cell egressCxcl12 transcriptionMarrow stromal cellsB cell retentionErythropoietin receptorBone marrow microenvironmentBone marrowHematopoietic stemB cellsPrecursor cellsPhenylhydrazine-induced hemolytic anemiaExpression levelsErythropoietin stimulationMesenchymal stromal cellsMarrow microenvironmentSingle methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions
He L, Steinocher H, Shelar A, Cohen EB, Heim EN, Kragelund BB, Grigoryan G, DiMaio D. Single methyl groups can act as toggle switches to specify transmembrane Protein-protein interactions. ELife 2017, 6: e27701. PMID: 28869036, PMCID: PMC5597333, DOI: 10.7554/elife.27701.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsErythropoietin receptorTransmembrane proteinTransmembrane protein-protein interactionsTMD interactionsModel transmembrane proteinMouse erythropoietin receptorHuman erythropoietin receptorSingle methyl groupGrowth factor independenceSide chain methyl groupsCellular processesMouse cellsFactor independenceChain methyl groupsIntrinsic specificityToggle switchTraptamersMethyl groupProteinReceptor activitySpecific positionsReceptorsSpecificityOligomerization
2008
The bovine papillomavirus E5 protein and the PDGF β receptor: It takes two to tango
Talbert-Slagle K, DiMaio D. The bovine papillomavirus E5 protein and the PDGF β receptor: It takes two to tango. Virology 2008, 384: 345-351. PMID: 18990418, PMCID: PMC2661243, DOI: 10.1016/j.virol.2008.09.033.Peer-Reviewed Original ResearchConceptsBovine papillomavirus E5 proteinE5 proteinTransmembrane domainTransmembrane proteinTarget proteinsPlatelet-derived growth factor beta receptorArtificial transmembrane proteinsMembrane-spanning segmentsHuman erythropoietin receptorBPV E5 proteinGrowth factor beta receptorCellular receptor tyrosine kinasesLigand-independent activationReceptor tyrosine kinasesGenetic screenPDGF β-receptorNovel proteinTransmembrane sequenceCellular proteinsMitogenic signalingHydrophobic proteinsReceptor dimerizationLarger target proteinsErythropoietin receptorSmall proteins
2001
The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*
Mendrola JM, Berger MB, King MC, Lemmon MA. The Single Transmembrane Domains of ErbB Receptors Self-associate in Cell Membranes*. Journal Of Biological Chemistry 2001, 277: 4704-4712. PMID: 11741943, DOI: 10.1074/jbc.m108681200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceCell MembraneChloramphenicol O-AcetyltransferaseDimerizationDNA Mutational AnalysisErbB ReceptorsEscherichia coliGenetic VectorsGlutamic AcidHumansLigandsMaltoseModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein Structure, TertiaryReceptor Protein-Tyrosine KinasesReceptor, ErbB-2Receptor, ErbB-3Receptor, ErbB-4Recombinant Fusion ProteinsSequence Homology, Amino AcidValineConceptsTM domain interactionsTM domainReceptor tyrosine kinasesEpidermal growth factor receptorGrowth factor receptorDomain interactionsSingle transmembrane alpha-helixReceptor dimersTyrosine kinaseExtracellular domainErbB receptor functionEscherichia coli cell membraneSingle transmembrane domainTransmembrane alpha-helixErbB receptorsCell membraneLimited mutational analysisFactor receptorGlutamic acid mutationTransmembrane domainGxxxG motifDomain dimerMutational analysisAlpha-helixErythropoietin receptor
1998
VIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways
DiMaio D, Lai C, Klein O. VIROCRINE TRANSFORMATION: The Intersection Between Viral Transforming Proteins and Cellular Signal Transduction Pathways. Annual Review Of Microbiology 1998, 52: 397-421. PMID: 9891803, DOI: 10.1146/annurev.micro.52.1.397.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, Polyomavirus TransformingBovine papillomavirus 1CattleCell Transformation, ViralHerpesvirus 4, HumanMiceOncogene ProteinsReceptor Protein-Tyrosine KinasesReceptor, Platelet-Derived Growth Factor betaReceptors, ErythropoietinReceptors, Platelet-Derived Growth FactorReceptors, Tumor Necrosis FactorSignal TransductionViral Envelope ProteinsViral Matrix ProteinsViral ProteinsConceptsCellular signal transduction pathwaysSignal transduction pathwaysTransduction pathwaysPlatelet-derived growth factor beta receptorPolyoma virus middle T antigenCellular signal transductionViral transforming proteinsCellular signaling pathwaysViral transformationMiddle T antigenGrowth factor beta receptorReceptor tyrosine kinasesTransforming proteinSignal transductionE5 proteinTumor necrosis factor receptorErythropoietin receptorTyrosine kinaseSignaling pathwaysCell transformationDiverse virusesNecrosis factor receptorViral oncoproteinsSpleen focusT antigen
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply