2017
Non-apoptotic functions of BCL-2 family proteins
Gross A, Katz SG. Non-apoptotic functions of BCL-2 family proteins. Cell Death & Differentiation 2017, 24: 1348-1358. PMID: 28234359, PMCID: PMC5520452, DOI: 10.1038/cdd.2017.22.Peer-Reviewed Original ResearchConceptsNon-apoptotic rolesBcl-2 family proteinsFamily proteinsApoptotic roleNon-apoptotic functionsWhole-cell metabolismCellular survival pathwaysMitochondrial physiologyCellular survivalSurvival pathwaysMajor regulatorNuclear processesApoptosis processProteinMechanism of actionPhysiologyImportant cluesRoleAutophagyRegulatorFascinating fieldRegulationPathwayMechanismMetabolism
2014
Distinct BimBH3 (BimSAHB) Stapled Peptides for Structural and Cellular Studies
Bird GH, Gavathiotis E, LaBelle JL, Katz SG, Walensky LD. Distinct BimBH3 (BimSAHB) Stapled Peptides for Structural and Cellular Studies. ACS Chemical Biology 2014, 9: 831-837. PMID: 24358963, PMCID: PMC4131438, DOI: 10.1021/cb4003305.Peer-Reviewed Original Research
2008
BAX activation is initiated at a novel interaction site
Gavathiotis E, Suzuki M, Davis ML, Pitter K, Bird GH, Katz SG, Tu HC, Kim H, Cheng E, Tjandra N, Walensky LD. BAX activation is initiated at a novel interaction site. Nature 2008, 455: 1076-1081. PMID: 18948948, PMCID: PMC2597110, DOI: 10.1038/nature07396.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApoptosisApoptosis Regulatory ProteinsBcl-2-Associated X ProteinBcl-2-Like Protein 11BH3 Interacting Domain Death Agonist ProteinCell LineGene Expression RegulationHumansMembrane ProteinsMiceMutagenesis, Site-DirectedMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProto-Oncogene ProteinsSequence AlignmentConceptsAnti-apoptotic proteinsInteraction sitesBax activationBax-mediated cell deathBCL-2 domainsCell deathBcl-2 familyNovel interaction sitePro-apoptotic proteinsPoint mutagenesisMitochondrial apoptosisBax interactionStress stimuliΑ-helixProteinNew targetsBaxTherapeutic modulationDirect activationActivation siteApoptosisActivationFunctional activitySitesMutagenesis
2007
Pharmacologic Replacement of BIM BH3 Reactivates Apoptosis in Hematologic Cancer and Lymphoproliferative Disease.
LaBelle J, Fisher J, Katz S, Bird G, Lawrence C, Silverstein A, Walensky L. Pharmacologic Replacement of BIM BH3 Reactivates Apoptosis in Hematologic Cancer and Lymphoproliferative Disease. Blood 2007, 110: 524. DOI: 10.1182/blood.v110.11.524.524.Peer-Reviewed Original ResearchAnti-apoptotic proteinsBim-/- miceBcl-2 family protein interactionsBCL-2 domainsBH3-only proteinsRegulation of apoptosisApoptotic signaling pathwaysPro-apoptotic proteinsPromising pharmacologic strategyAnti-apoptotic targetsCellular homeostasisBH3 domainProtein interactionsDeath pathwaysProtein networkCellular survivalSignaling pathwaysApoptotic blockadesCell deathSAHBLymphoma cell linesBH3Apoptosis inductionProteinMitochondrial damage
2002
Interaction between FOG-1 and the Corepressor C-Terminal Binding Protein Is Dispensable for Normal Erythropoiesis In Vivo
Katz SG, Cantor AB, Orkin SH. Interaction between FOG-1 and the Corepressor C-Terminal Binding Protein Is Dispensable for Normal Erythropoiesis In Vivo. Molecular And Cellular Biology 2002, 22: 3121-3128. PMID: 11940669, PMCID: PMC133767, DOI: 10.1128/mcb.22.9.3121-3128.2002.Peer-Reviewed Original ResearchMeSH KeywordsAlcohol OxidoreductasesAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesBlotting, WesternCarrier ProteinsCell LineConserved SequenceCOS CellsDNA-Binding ProteinsErythrocytesErythropoiesisErythropoietinGenetic VectorsHematocritMiceMice, KnockoutMutationNuclear ProteinsPhenylhydrazinesPhosphoproteinsPrecipitin TestsProtein BindingRepressor ProteinsSequence Homology, Amino AcidTranscription FactorsTransgenesConceptsC-terminal binding proteinFOG-1Corepressor C-terminal binding proteinTranscription factor GATA-1Binding proteinCorepressor CtBPCtBP interactsErythroid developmentGATA-1Vivo functionCtBPMegakaryocytic lineagePeptide motifsPhysiological roleInteraction sitesNormal erythropoiesisErythropoietic stressCell linesStages of developmentProteinErythrocyte productionFamily membersWild-type miceErythropoiesisCoimmunoprecipitation
2001
Friend of GATA-1 Represses GATA-3–dependent Activity in CD4+ T Cells
Zhou M, Ouyang W, Gong Q, Katz S, White J, Orkin S, Murphy K. Friend of GATA-1 Represses GATA-3–dependent Activity in CD4+ T Cells. Journal Of Experimental Medicine 2001, 194: 1461-1471. PMID: 11714753, PMCID: PMC2193678, DOI: 10.1084/jem.194.10.1461.Peer-Reviewed Original ResearchConceptsFOG-1Friend of GATATranscription factor activityActivator of transcriptionIL-5 promoterHematopoietic developmentMegakaryocyte differentiationSignal transducerGATA-3Dependent inductionFactor activityNaive T cellsTh2 developmentT cellsOverexpressionAutoactivationCellsGATA-3 expressionPrimary activationActivationInductionTranscriptionPromoterGATAProtein