2016
Loss of TRIM33 causes resistance to BET bromodomain inhibitors through MYC- and TGF-β–dependent mechanisms
Shi X, Mihaylova VT, Kuruvilla L, Chen F, Viviano S, Baldassarre M, Sperandio D, Martinez R, Yue P, Bates JG, Breckenridge DG, Schlessinger J, Turk BE, Calderwood DA. Loss of TRIM33 causes resistance to BET bromodomain inhibitors through MYC- and TGF-β–dependent mechanisms. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e4558-e4566. PMID: 27432991, PMCID: PMC4978292, DOI: 10.1073/pnas.1608319113.Peer-Reviewed Original ResearchMeSH KeywordsAzepinesCell Line, TumorCell ProliferationColorectal NeoplasmsDrug ResistanceGene Expression Regulation, NeoplasticHCT116 CellsHEK293 CellsHumansMolecular StructureProteinsProto-Oncogene Proteins c-mycReceptors, Transforming Growth Factor betaRNA InterferenceSignal TransductionTranscription FactorsTransforming Growth Factor betaTriazolesConceptsTGF-β receptor activityExtraterminal domain protein inhibitorsRegulation of MYCCancer cellsBET bromodomain inhibitionShRNA screeningProtein 33TGF-β receptor expressionBromodomain inhibitorsProtein inhibitorInhibition of TGFColorectal cancer cellsBromodomain inhibitionBETi resistanceCancer therapeuticsNew therapeutic benefitsDurable responsesMYCDependent mechanismReceptor expressionTherapeutic benefitBETiReceptor activityResistant stateAntiproliferative effects
2015
CCM2–CCM3 interaction stabilizes their protein expression and permits endothelial network formation
Draheim KM, Li X, Zhang R, Fisher OS, Villari G, Boggon TJ, Calderwood DA. CCM2–CCM3 interaction stabilizes their protein expression and permits endothelial network formation. Journal Of Cell Biology 2015, 208: 987-1001. PMID: 25825518, PMCID: PMC4384732, DOI: 10.1083/jcb.201407129.Peer-Reviewed Original ResearchMeSH KeywordsApoptosis Regulatory ProteinsBinding SitesCarrier ProteinsCell LineCell ProliferationCentral Nervous SystemCrystallography, X-RayGene ExpressionHemangioma, Cavernous, Central Nervous SystemHumansMembrane ProteinsMutagenesisNeovascularization, PhysiologicPaxillinProtein BindingProtein Interaction MappingProtein Structure, TertiaryProteolysisProto-Oncogene ProteinsRNA InterferenceRNA, Small InterferingSequence AlignmentConceptsBinding-deficient mutantStructure-guided mutagenesisNormal cell growthCerebral cavernous malformationsEndothelial network formationHomology domainCCM3 proteinsProteasomal degradationEndothelial cell network formationMolecular basisCell network formationEssential adaptorCell growthFunctional significanceCCM3 expressionX-ray crystallographyProtein expressionCCM2CCM3Network formationExpressionMutantsHP1MutagenesisAdaptor
2009
The E3 ubiquitin ligase specificity subunit ASB2β is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation
Bello NF, Lamsoul I, Heuzé ML, Métais A, Moreaux G, Calderwood DA, Duprez D, Moog-Lutz C, Lutz PG. The E3 ubiquitin ligase specificity subunit ASB2β is a novel regulator of muscle differentiation that targets filamin B to proteasomal degradation. Cell Death & Differentiation 2009, 16: 921-932. PMID: 19300455, PMCID: PMC2709956, DOI: 10.1038/cdd.2009.27.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCarrier ProteinsCell DifferentiationCell LineChickensContractile ProteinsFilaminsGene Knockdown TechniquesHumansMiceMicrofilament ProteinsMyoblastsProteasome Endopeptidase ComplexRNA InterferenceRNA, MessengerSuppressor of Cytokine Signaling ProteinsUbiquitin-Protein LigasesConceptsFilamin BMuscle differentiationSpecificity subunitAnkyrin repeat-containing proteinActive E3 ubiquitin ligaseE3 ubiquitin ligase complexRepeat-containing proteinUbiquitin ligase complexE3 ubiquitin ligaseSuppressor of cytokineBox 2 geneLigase complexE3 ubiquitinUbiquitin ligaseProteasomal degradationMyoblast fusionNovel regulatorMuscle developmentKnockdown cellsProtein degradationMyogenic differentiationAdult tissuesC2C12 cellsMuscle contractile proteinsInduced differentiation
2004
Talin controls integrin activation
Calderwood DA. Talin controls integrin activation. Biochemical Society Transactions 2004, 32: 434-437. PMID: 15157154, DOI: 10.1042/bst0320434.Peer-Reviewed Original ResearchConceptsIntegrin beta tailsIntegrin activationCytoplasmic domainBeta tailsMajor actin-binding proteinIntegrin beta cytoplasmic domainsBeta cytoplasmic domainsIntegrin cytoplasmic domainIntegrin activation pathwaysCytoskeletal protein talinIntegrin extracellular domainActin-binding proteinsIntegrin adhesion receptorsBinding of talinTalin FERM domainIntegrin-binding siteMulticellular organismsPTB domainFERM domainProtein talinExtracellular ligandsTalin expressionRNA interferenceTalinIntracellular signals