2024
Ezrin drives adaptation of monocytes to the inflamed lung microenvironment
Gudneppanavar R, Di Pietro C, H Öz H, Zhang P, Cheng E, Huang P, Tebaldi T, Biancon G, Halene S, Hoppe A, Kim C, Gonzalez A, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. Cell Death & Disease 2024, 15: 864. PMID: 39613751, PMCID: PMC11607083, DOI: 10.1038/s41419-024-07255-8.Peer-Reviewed Original ResearchConceptsActivation of focal adhesion kinaseExtracellular matrixActin-binding proteinsFocal adhesion kinaseLung extracellular matrixKnock-out mouse modelProtein kinase signalingCortical cytoskeletonLoss of ezrinKinase signalingPlasma membraneCell migrationSignaling pathwayEzrinResponse to lipopolysaccharideTissue-resident macrophagesMouse modelLipopolysaccharideCytoskeletonEzrin expressionLung microenvironmentKinaseMonocyte recruitmentProteinAktPKCδ-Mediated Phosphorylation of CD25 Initiates Feedback Control of Oncogenic Tyrosine Kinases in Acute Lymphoblastic Leukemia
Sun R, Lee J, Artadji D, Robinson M, Kume K, Cheng Z, Cosgun K, Chan L, Leveille E, Ma N, Geng H, Paietta E, Vaidehi N, Müschen M. PKCδ-Mediated Phosphorylation of CD25 Initiates Feedback Control of Oncogenic Tyrosine Kinases in Acute Lymphoblastic Leukemia. Blood 2024, 144: 632-632. DOI: 10.1182/blood-2024-211038.Peer-Reviewed Original ResearchB-ALL cellsPatient-derived xenograftsPh+ B-ALLPh-like B-ALLAntibody-drug conjugatesB-ALL casesB-ALLCre-mediated deletionOncogenic tyrosine kinasesBCR-ABL1Tyrosine kinase signalingSurface expressionColony formation capacityCD25 mRNACell surface expression of CD25Tyrosine kinaseGenetic deletionSurface expression of CD25Oncogenic tyrosine kinase signalingKinase signalingOncogene BCR-ABL1Transplant recipient miceControl ADCNegative feedback regulationExpression of CD25
2023
Theoretical analysis reveals a role for RAF conformational autoinhibition in paradoxical activation
Mendiratta G, Stites E. Theoretical analysis reveals a role for RAF conformational autoinhibition in paradoxical activation. ELife 2023, 12: e82739. PMID: 37823369, PMCID: PMC10627510, DOI: 10.7554/elife.82739.Peer-Reviewed Original ResearchMulti-omics profiling reveals cellular pathways and functions regulated by ALDH1B1 in colon cancer cells
Wang Y, Popovic Z, Charkoftaki G, Garcia-Milian R, Lam T, Thompson D, Chen Y, Vasiliou V. Multi-omics profiling reveals cellular pathways and functions regulated by ALDH1B1 in colon cancer cells. Chemico-Biological Interactions 2023, 384: 110714. PMID: 37716420, PMCID: PMC10807983, DOI: 10.1016/j.cbi.2023.110714.Peer-Reviewed Original ResearchColon cancer cellsCellular stress response pathwaysStress response pathwaysMulti-omics analysisCancer cellsSecond messenger signalingMulti-omics profilingNew molecular informationFunctional annotationCellular functionsResponse pathwaysKinase signalingCellular pathwaysColon adenocarcinoma cell lineHuman colon adenocarcinoma cell lineApoptosis signalingEnrichment analysisAldehyde dehydrogenase 1B1Molecular signaturesAdenocarcinoma cell lineMolecular informationSignalingNovel targetProtein expressionCell lines
2019
The Psychiatric Risk Gene NT5C2 Regulates Adenosine Monophosphate-Activated Protein Kinase Signaling and Protein Translation in Human Neural Progenitor Cells
Duarte RRR, Bachtel ND, Côtel MC, Lee SH, Selvackadunco S, Watson IA, Hovsepian GA, Troakes C, Breen GD, Nixon DF, Murray RM, Bray NJ, Eleftherianos I, Vernon AC, Powell TR, Srivastava DP. The Psychiatric Risk Gene NT5C2 Regulates Adenosine Monophosphate-Activated Protein Kinase Signaling and Protein Translation in Human Neural Progenitor Cells. Biological Psychiatry 2019, 86: 120-130. PMID: 31097295, PMCID: PMC6614717, DOI: 10.1016/j.biopsych.2019.03.977.Peer-Reviewed Original ResearchConceptsHuman neural progenitor cellsProtein translationNeural progenitor cellsMotility behaviorAvailable expression dataRibosomal protein S6Protein Kinase SignalingRegulation of AMPKProgenitor cellsNutrient sensing mechanismsProtein kinase alphaQuantitative polymerase chain reactionPsychiatric risk allelesDrosophila melanogasterTranscriptional changesKinase signalingProtein S6Transcriptomic profilingRNA interferenceNeural stem cellsExpression changesKinase alphaUnknown roleExpression dataHuman dorsolateral prefrontal cortex
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
2014
The docking protein FRS2α is a critical regulator of VEGF receptors signaling
Chen PY, Qin L, Zhuang ZW, Tellides G, Lax I, Schlessinger J, Simons M. The docking protein FRS2α is a critical regulator of VEGF receptors signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 5514-5519. PMID: 24706887, PMCID: PMC3992672, DOI: 10.1073/pnas.1404545111.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCell MovementDNA PrimersEndothelial CellsGene Expression ProfilingGenetic VectorsHEK293 CellsHuman Umbilical Vein Endothelial CellsHumansImmunoblottingImmunohistochemistryImmunoprecipitationLaser-Doppler FlowmetryLentivirusMembrane ProteinsMiceReal-Time Polymerase Chain ReactionReceptors, Vascular Endothelial Growth FactorSignal TransductionX-Ray MicrotomographyConceptsLymphatic endothelial cell migrationFibroblast growth factor receptor substrate 2Growth factor receptor substrate 2Cognate receptor tyrosine kinasesFactor receptor substrate 2Receptor kinase signalingVascular endothelial growth factorPostnatal vascular developmentReceptor tyrosine kinasesEndothelial cell migrationKinase signalingEndothelial-specific deletionAdult angiogenesisVEGF receptorsTyrosine kinaseCritical regulatorVascular developmentFRS2αSubstrate 2Cell migrationDependent activationCritical roleUnidentified componentsGrowth factorEndothelial growth factor
2011
Targeting Inhibitory Phosphatases in Tyrosine Kinase-Driven Leukemias
Shojaee S, Buchner M, Geng H, Silvia B, Koeffler P, Muschen M. Targeting Inhibitory Phosphatases in Tyrosine Kinase-Driven Leukemias. Blood 2011, 118: 1382. DOI: 10.1182/blood.v118.21.1382.1382.Peer-Reviewed Original ResearchCell deathReactive oxygen speciesInducible deletionLeukemia cellsTyrosine kinase signalingActivation signalsSmall molecule inhibitionSubsequent cell deathMultiple new targetsLeukemia cell deathBCR-ABL1 oncogeneCytoplasmic tailKinase signalingTransplant recipient miceInduction of CreTyrosine kinase inhibitorsCellular senescenceMolecule inhibitionTyrosine kinasePTPN6Drastic upregulationINPP5DCurrent tyrosine kinase inhibitorsPTENDeletion
2009
Targeting extracellular signal-regulated kinase (ERK) signaling has therapeutic implications for inflammatory osteolysis
Seo SW, Lee D, Minematsu H, Kim AD, Shin M, Cho SK, Kim DW, Yang J, Lee FY. Targeting extracellular signal-regulated kinase (ERK) signaling has therapeutic implications for inflammatory osteolysis. Bone 2009, 46: 695-702. PMID: 19895919, PMCID: PMC2823832, DOI: 10.1016/j.bone.2009.10.032.Peer-Reviewed Original ResearchConceptsInflammatory osteolysisInflammatory responseInnate immune responseExtracellular signal-regulated kinase (ERK) signalingImportant therapeutic targetM-CSF expressionSignal-regulated kinase 1/2 pathwaySignal-regulated kinase signalingExtracellular signal-regulated kinase 1/2 (ERK1/2) pathwayInhibition of ERKImmune responseTherapeutic implicationsTherapeutic targetOsteoclast precursorsKinase 1/2 pathwayM-CSFOsteolysisERK pathwayMacrophage colonyLPSERKERK signalsMitogen-activated protein kinase (MAPK) familyKinase signalingCell differentiationThe Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site
Bae J, Lew E, Yuzawa S, Tomé F, Lax I, Schlessinger J. The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site. Journal Of End-to-End-testing 2009, 138: 514-524. DOI: 10.1016/s9999-9994(09)20438-7.Peer-Reviewed Original ResearchSH2 domainSH2 domain-mediated interactionsReceptor tyrosine kinase signalingPhosphorylation-independent mannerReceptor phosphorylation sitesDomain-mediated interactionsDomain Binding SiteSpecific cellular processesTyrosine kinase signalingParticular sequence motifsReceptor tyrosine kinasesBinding sitesTyrosine kinase domainPhosphorylation sitesCellular processesSequence motifsKinase signalingKinase domainPhospholipase CγTyrosine kinaseSecondary binding siteCultured cellsDomain selectivityRegulation of selectivityIndependent mannerThe Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site
Bae JH, Lew ED, Yuzawa S, Tomé F, Lax I, Schlessinger J. The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site. Cell 2009, 138: 514-524. PMID: 19665973, PMCID: PMC4764080, DOI: 10.1016/j.cell.2009.05.028.Peer-Reviewed Original ResearchConceptsSH2 domainSH2 domain-mediated interactionsReceptor tyrosine kinase signalingPhosphorylation-independent mannerReceptor phosphorylation sitesDomain-mediated interactionsDomain Binding SiteSpecific cellular processesTyrosine kinase signalingParticular sequence motifsReceptor tyrosine kinasesBinding sitesTyrosine kinase domainPhosphorylation sitesCellular processesSequence motifsPhospholipase CgammaKinase signalingKinase domainTyrosine kinaseSecondary binding siteCultured cellsDomain selectivityRegulation of selectivityIndependent manner
2007
Dissecting kinase signaling pathways
Boyle SN, Koleske AJ. Dissecting kinase signaling pathways. Drug Discovery Today 2007, 12: 717-724. PMID: 17826684, DOI: 10.1016/j.drudis.2007.07.019.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedAntineoplastic AgentsBenzamidesDrug Delivery SystemsHumansImatinib MesylateLapatinibNeoplasmsPhosphoproteinsPhosphorylationPiperazinesProtein Kinase InhibitorsProtein KinasesProteomicsPyrimidinesQuinazolinesSignal TransductionTrastuzumabConceptsSame protein substrateProtein Kinase SignalingKinase substratePutative substratesProtein substratesKinase signalingProtein kinaseMultiple kinasesPhysiological substratesKinaseHuman diseasesDrug targetsPhysiological relevanceSubstrate interactionsKinase inhibitorsPathwaySignalingSubstrateNeurological disordersInteractionHallmarkInhibitorsTargetLow-Dose BBR3610 Toxicity in Colon Cancer Cells Is p53-Independent and Enhanced by Inhibition of Epidermal Growth Factor Receptor (ERBB1)-Phosphatidyl Inositol 3 Kinase Signaling
Mitchell C, Kabolizadeh P, Ryan J, Roberts JD, Yacoub A, Curiel DT, Fisher PB, Hagan MP, Farrell NP, Grant S, Dent P. Low-Dose BBR3610 Toxicity in Colon Cancer Cells Is p53-Independent and Enhanced by Inhibition of Epidermal Growth Factor Receptor (ERBB1)-Phosphatidyl Inositol 3 Kinase Signaling. Molecular Pharmacology 2007, 72: 704-714. PMID: 17578896, DOI: 10.1124/mol.107.038406.Peer-Reviewed Original ResearchConceptsColon cancer cellsEpidermal growth factor receptorGrowth factor receptorActive AktC-FLIPMolecular inhibitionCaspase-8 functionsPhosphatidyl inositol 3 kinaseActivation of BaxDominant-negative AktErbB1 inhibitorsFactor receptorHuman colon cancer cellsOverexpression of XIAPCancer cellsSmall moleculesKinase signalingPI3K inhibitorsAkt activityCaspase-9Bcl-xLNull cellsMcl-1SW480 cellsK-RASLack of Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase Signaling Shows a New Type of Melanoma
Shields JM, Thomas NE, Cregger M, Berger AJ, Leslie M, Torrice C, Hao H, Penland S, Arbiser J, Scott G, Zhou T, Bar-Eli M, Bear JE, Der CJ, Kaufmann WK, Rimm DL, Sharpless NE. Lack of Extracellular Signal-Regulated Kinase Mitogen-Activated Protein Kinase Signaling Shows a New Type of Melanoma. Cancer Research 2007, 67: 1502-1512. PMID: 17308088, DOI: 10.1158/0008-5472.can-06-3311.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseERK activationB-RafERK activityMitogen-Activated Protein Kinase SignalingSignal-regulated kinase kinaseN-RASERK MAPK cascadeProtein Kinase SignalingPrimary human melanocytesRNA expression profilesCell linesEpithelial-mesenchymal transformationDistinct melanoma subtypeMAPK cascadeKinase kinaseExtracellular signalsTranscriptional targetsKinase signalingProtein kinaseExpression profilesEpithelial markersMelanoma cell linesRAS/RAFPrimary human tumorsEmploying Systems Biology to Quantify Receptor Tyrosine Kinase Signaling in Time and Space
Kholodenko B. Employing Systems Biology to Quantify Receptor Tyrosine Kinase Signaling in Time and Space. 2007, 300-318. DOI: 10.1007/978-1-59745-531-2_16.Peer-Reviewed Original ResearchProtein phosphorylation networksReceptor tyrosine kinase signalingTrafficking of endosomesPivotal physiological processesTyrosine kinase signalingPlasma membrane receptorsPhosphorylation networksUltrasensitive switchPhosphorylated kinasesKinase signalingEnvironmental cuesCell motilitySystems biologyNegative feedback circuitPhysiological processesCellular responsesMembrane receptorsLiving cellsCellular architectureSpatiotemporal response patternsComputational approachIntricate relationshipEndosomesKinaseMitosis
2006
The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala
Paul S, Olausson P, Venkitaramani DV, Ruchkina I, Moran TD, Tronson N, Mills E, Hakim S, Salter MW, Taylor JR, Lombroso PJ. The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala. Biological Psychiatry 2006, 61: 1049-1061. PMID: 17081505, PMCID: PMC1853327, DOI: 10.1016/j.biopsych.2006.08.005.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAminoacetonitrileAmygdalaAnimalsBehavior, AnimalCells, CulturedConditioning, ClassicalCycloheximideElectric StimulationEnzyme InhibitorsFearFemaleImmunohistochemistryIn Vitro TechniquesLong-Term PotentiationMemoryMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeostriatumPatch-Clamp TechniquesPoint MutationPregnancyProtein Synthesis InhibitorsProtein Tyrosine PhosphatasesRatsRats, Sprague-DawleyTranslocation, GeneticConceptsStriatal-enriched protein tyrosine phosphataseERK1/2 activationMitogen-activated protein kinaseProtein tyrosine phosphataseDe novo translationActivation of ERK1/2Tyrosine phosphataseProtein bindsKinase signalingProtein kinaseSequential recruitmentAmygdala-dependent memory formationERK pathwayMemory formationPrimary cell culturesNuclear translocationBiphasic activationLong-term potentiationTranslation blockTAT-STEPERKCell culturesERK1/2ActivationPathwayP-393 C-Jun N-terminal kinase (JNK) signaling regulates cell proliferation and apoptosis in endometrial cells
Kizilay G, Basar M, Cakmak H, Atabekoglu C, Kayisli U, Arici A. P-393 C-Jun N-terminal kinase (JNK) signaling regulates cell proliferation and apoptosis in endometrial cells. Fertility And Sterility 2006, 86: s281. DOI: 10.1016/j.fertnstert.2006.07.750.Peer-Reviewed Original Research
2000
Visualizing protein dynamics in yeast with green fluorescent protein
Burd C. Visualizing protein dynamics in yeast with green fluorescent protein. Methods In Enzymology 2000, 327: 61-69. PMID: 11044974, DOI: 10.1016/s0076-6879(00)27267-4.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein dynamicsUse of GFPFluorescent proteinYeast cell biologyProtein sortingRNA localizationIndividual cellular componentsChromosomal dynamicsProtein localizationKinase signalingCell biologyMutant strainMolecular tagsCellular componentsYeastProteinNucleocytoplasmicBroad arrayLocalizationSignalingBiologySortingMajor impactTags
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