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 differentiationThe Role of FilGAP-Filamin A Interactions in Mechanoprotection
Shifrin Y, Arora PD, Ohta Y, Calderwood DA, McCulloch CA. The Role of FilGAP-Filamin A Interactions in Mechanoprotection. Molecular Biology Of The Cell 2009, 20: 1269-1279. PMID: 19144823, PMCID: PMC2649276, DOI: 10.1091/mbc.e08-08-0872.Peer-Reviewed Original Research
2008
JAM-L–mediated leukocyte adhesion to endothelial cells is regulated in cis by α4β1 integrin activation
Luissint AC, Lutz PG, Calderwood DA, Couraud PO, Bourdoulous S. JAM-L–mediated leukocyte adhesion to endothelial cells is regulated in cis by α4β1 integrin activation. Journal Of Cell Biology 2008, 183: 1159-1173. PMID: 19064666, PMCID: PMC2600739, DOI: 10.1083/jcb.200805061.Peer-Reviewed Original ResearchConceptsJunctional adhesion moleculeIntegrin activationIntegrin-dependent adhesionIntegrin VLA-4Endothelial cellsAdhesion moleculesEpithelial adhesion moleculesJAM familyHeterophilic interactionsCis dimerizationDimerization stateVLA-4Monomeric formLeukocyte integrin VLA-4CellsActivationAdhesionComplexesProteinMoleculesDimerizationLeukocyte adhesionRecruitmentAccumulationFamily
2003
The Kindler Syndrome Protein Is Regulated by Transforming Growth Factor-β and Involved in Integrin-mediated Adhesion*
Kloeker S, Major MB, Calderwood DA, Ginsberg MH, Jones DA, Beckerle MC. The Kindler Syndrome Protein Is Regulated by Transforming Growth Factor-β and Involved in Integrin-mediated Adhesion*. Journal Of Biological Chemistry 2003, 279: 6824-6833. PMID: 14634021, DOI: 10.1074/jbc.m307978200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceBlotting, NorthernBlotting, WesternCell AdhesionCell LineCell MovementCytoplasmCytoskeletonDisease ProgressionDNA, ComplementaryExtracellular Matrix ProteinsFluorescent Antibody Technique, IndirectGene Expression RegulationHumansIntegrin beta1Integrin beta3IntegrinsMembrane ProteinsModels, MolecularMolecular Sequence DataMutationNeoplasm ProteinsOligonucleotide Array Sequence AnalysisProtein BindingProtein Structure, TertiaryRNARNA, MessengerRNA, Small InterferingSequence Homology, Amino AcidTime FactorsTransfectionTransforming Growth Factor betaUp-RegulationConceptsHuman mammary epithelial cellsCytoplasmic domainIntegrin cytoplasmic domainBeta3 integrin cytoplasmic domainsCDNA microarray analysisTGF-beta stimulationNormal cell spreadingMammary epithelial cellsSyndrome proteinFERM domainFocal adhesionsTranscriptional profilesProtein abundanceCritical residuesMicroarray analysisCell spreadingGene leadTalin-FERMCell migrationCancer progressionIntegrin betaGenesCell processesAutosomal recessive genodermatosisEpithelial cellsTalin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation
Tadokoro S, Shattil SJ, Eto K, Tai V, Liddington RC, de Pereda J, Ginsberg MH, Calderwood DA. Talin Binding to Integrin ß Tails: A Final Common Step in Integrin Activation. Science 2003, 302: 103-106. PMID: 14526080, DOI: 10.1126/science.1086652.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionAnimalsAntibodies, MonoclonalCell LineFibronectinsHumansIntegrin beta ChainsIntegrin beta1Integrin beta3Molecular Sequence DataMutationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein ConformationProtein Structure, TertiaryRecombinant ProteinsRNA, Small InterferingSignal TransductionTalinTransfectionConceptsIntegrin activationCytoplasmic tailIntegrin betaCytoskeletal protein talinIntegrin extracellular domainCellular signaling cascadesIntegrin beta tailsNormal cell adhesionBinding of talinProtein talinBeta tailsSignaling cascadesIntegrin affinityConformational rearrangementsExtracellular domainFinal common stepTalinCell adhesionExtracellular matrixCommon stepSpecific bindingActivationBindingTailAffinity
2000
Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport*
Fenczik C, Zent R, Dellos M, Calderwood D, Satriano J, Kelly C, Ginsberg M. Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport*. Journal Of Biological Chemistry 2000, 276: 8746-8752. PMID: 11121428, DOI: 10.1074/jbc.m011239200.Peer-Reviewed Original ResearchConceptsAmino acid transportIntegrin functionAcid transportDistinct domainsType II transmembrane proteinIsoleucine transportAmino acid transportersCD98 heavy chainCell surface heterodimersTransmembrane domainCytoplasmic domainTransmembrane proteinSurface heterodimersExtracellular domainAcid transportersCD98hcHeavy chainProteinIntegrinsCovalent linkageDifferent light chainsLight chainDomainMutantsHeterodimersClass- and Splice Variant-specific Association of CD98 with Integrin β Cytoplasmic Domains*
Zent R, Fenczik C, Calderwood D, Liu S, Dellos M, Ginsberg M. Class- and Splice Variant-specific Association of CD98 with Integrin β Cytoplasmic Domains*. Journal Of Biological Chemistry 2000, 275: 5059-5064. PMID: 10671548, DOI: 10.1074/jbc.275.7.5059.Peer-Reviewed Original ResearchConceptsCytoplasmic domainIntegrin activationMuscle-specific splice variantIntegrin beta cytoplasmic domainsBasic amino acid transportType II transmembrane proteinIntegrin β cytoplasmic domainBeta cytoplasmic domainsIntegrin cytoplasmic domainCell fusion eventsIntegrin adhesion receptorsAmino acid transportTransmembrane proteinMembrane proteinsFusion eventsIntegrin classAdhesion receptorsSplice variantsAcid transportCD98Variant specificityProteinIntegrinsDomainActivation