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
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
2012
A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers
LaBelle JL, Katz SG, Bird GH, Gavathiotis E, Stewart ML, Lawrence C, Fisher JK, Godes M, Pitter K, Kung AL, Walensky LD. A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers. Journal Of Clinical Investigation 2012, 122: 2018-2031. PMID: 22622039, PMCID: PMC3366394, DOI: 10.1172/jci46231.Peer-Reviewed Original ResearchConceptsBcl-2 family proteinsCell deathFamily proteinsPro-apoptotic Bcl-2 family proteinsBcl-2 protein familyBcl-2-interacting mediatorBcl-2 family pathwayHydrocarbon-stapled peptidesCell death mechanismsCancer cellsCellular lifeHematologic cancer cellsProtein familyDeath domainBH3 helixBim BH3Bim peptidesDeath mechanismsApoptotic blockadesApoptotic resistanceFamily pathwaySurvival pathwaysAntiapoptotic proteinsProapoptotic activityHuman AML xenograft model
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 assays