2015
BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress
Carpio MA, Michaud M, Zhou W, Fisher JK, Walensky LD, Katz SG. BCL-2 family member BOK promotes apoptosis in response to endoplasmic reticulum stress. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 7201-7206. PMID: 26015568, PMCID: PMC4466744, DOI: 10.1073/pnas.1421063112.Peer-Reviewed Original ResearchConceptsB-cell lymphoma 2 ovarian killerApoptotic defectsMultidomain proapoptotic proteins BaxApoptotic responseStress stimuliER stressBcl-2 family proteinsER stress agentsUnfolded protein responseMouse embryonic fibroblastsDefective apoptotic responseMitochondrial apoptotic pathwayProapoptotic protein BaxPredominant subcellular localizationThapsigargin-induced apoptosisEndoplasmic reticulum stressFamily proteinsDeath responseSubcellular localizationEmbryonic fibroblastsHigh homologyProtein responseApoptotic pathwayOvert phenotypeProtein Bax
2008
Structural Analysis of a BAX-BIM SAHB Complex Reveals a Novel BH3 Interaction Site on BAX for Therapeutic Activation of Apoptosis
Gavathiotis E, Suzuki M, Davis M, Pitter K, Bird G, Katz S, Tu H, Kim H, Cheng E, Tjandra N, Walensky L. Structural Analysis of a BAX-BIM SAHB Complex Reveals a Novel BH3 Interaction Site on BAX for Therapeutic Activation of Apoptosis. Blood 2008, 112: 300. DOI: 10.1182/blood.v112.11.300.300.Peer-Reviewed Original ResearchAnti-apoptotic proteinsBax activationCell deathInteraction sitesAlpha-helixBCL-2 domainsBcl-2 family proteinsBcl-2 familyPathologic cell deathBax-mediated apoptosisFirst structural analysisPro-apoptotic proteinsDomain proteinsFamily proteinsMitochondrial translocationProtein interactionsPoint mutagenesisMitochondrial apoptosisStress stimuliBcl-xLConformational changesCell survivalMitochondrial dysfunctionNovel siteDistinct assaysBAX 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