2020
Signalling through cerebral cavernous malformation protein networks
Su VL, Calderwood DA. Signalling through cerebral cavernous malformation protein networks. Open Biology 2020, 10: 200263. PMID: 33234067, PMCID: PMC7729028, DOI: 10.1098/rsob.200263.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiomarkersCarrier ProteinsDisease ManagementDisease SusceptibilityGenetic Predisposition to DiseaseHemangioma, Cavernous, Central Nervous SystemHumansIntracellular SpaceMutationProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingProtein Interaction MapsProtein TransportSignal TransductionConceptsCCM proteinsCerebral cavernous malformationsCell junctionalMEKK3-MEK5Protein complexesAdaptor proteinProtein functionSubcellular localizationCytoskeletal reorganizationComplex proteinsProtein networkRhoA-ROCKMolecular basisProtein activityGene expressionFunction mutationsCell adhesionCell contractilityProteinPathwayLeaky blood vesselsCurrent knowledgeDisease pathologyCdc42Recent advances
2019
Coarse-Grained Simulation of Full-Length Integrin Activation
Bidone TC, Polley A, Jin J, Driscoll T, Iwamoto DV, Calderwood DA, Schwartz MA, Voth GA. Coarse-Grained Simulation of Full-Length Integrin Activation. Biophysical Journal 2019, 116: 1000-1010. PMID: 30851876, PMCID: PMC6428961, DOI: 10.1016/j.bpj.2019.02.011.Peer-Reviewed Original Research
2013
ASB2α, an E3 Ubiquitin Ligase Specificity Subunit, Regulates Cell Spreading and Triggers Proteasomal Degradation of Filamins by Targeting the Filamin Calponin Homology 1 Domain*
Razinia Z, Baldassarre M, Cantelli G, Calderwood DA. ASB2α, an E3 Ubiquitin Ligase Specificity Subunit, Regulates Cell Spreading and Triggers Proteasomal Degradation of Filamins by Targeting the Filamin Calponin Homology 1 Domain*. Journal Of Biological Chemistry 2013, 288: 32093-32105. PMID: 24052262, PMCID: PMC3814802, DOI: 10.1074/jbc.m113.496604.Peer-Reviewed Original ResearchConceptsHematopoietic cell differentiationSpecificity subunitProteasomal degradationF-actin-rich structuresE3 ubiquitin ligase complexCell differentiationNormal subcellular localizationHomology 1 domainLoss of filaminUbiquitin acceptor sitesActin-binding domainCross-linking proteinsActin-binding siteLigase complexActin cytoskeletonTransmembrane proteinSubcellular localizationΑ-actinin1Transient expressionASB2αDegradation of filaminMinimal fragmentLysine residuesFilaminCell adhesion
2009
Filamins Regulate Cell Spreading and Initiation of Cell Migration
Baldassarre M, Razinia Z, Burande CF, Lamsoul I, Lutz PG, Calderwood DA. Filamins Regulate Cell Spreading and Initiation of Cell Migration. PLOS ONE 2009, 4: e7830. PMID: 19915675, PMCID: PMC2773003, DOI: 10.1371/journal.pone.0007830.Peer-Reviewed Original ResearchConceptsCell spreadingLarge actin-binding proteinCell biological analysesCell migrationActin-binding proteinsLoss of FlnAShRNA-mediated knockdownInitiation of migrationInhibition of initiationRecent knockout studiesProteasomal degradationKnockdown cellsInitiation of motilityKnockout studiesFilaminSingle knockoutImpairs migrationFLNAFLNBBiological analysisKnockdownProteinObserved defectsCellsPeriventricular heterotopia
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 bindingActivationBindingTailAffinityIntegrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling
Calderwood DA, Fujioka Y, de Pereda JM, García-Alvarez B, Nakamoto T, Margolis B, McGlade CJ, Liddington RC, Ginsberg MH. Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 2272-2277. PMID: 12606711, PMCID: PMC151330, DOI: 10.1073/pnas.262791999.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDatabases as TopicDNADose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelGlutathione TransferaseHumansIntegrin beta ChainsIntegrinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationPhosphorylationPhosphotyrosinePrecipitin TestsProtein BindingProtein ConformationProtein Structure, TertiaryRecombinant Fusion ProteinsRecombinant ProteinsSequence Homology, Amino AcidSignal TransductionTransfectionTyrosineConceptsIntegrin beta tailsBeta tailsPTB domainIntegrin tailsDok-1Heterodimeric integrin adhesion receptorsBiological functionsDomain interactionsPTB domain-containing proteinsDomain-containing proteinsDomain-ligand interactionsPhosphotyrosine-binding (PTB) domainPhosphotyrosine-binding domainCytoplasmic domain interactionsIntegrin-binding proteinsIntegrin adhesion receptorsIntegrin alpha IIbNPXY motifProtein modulesCytoplasmic domainCytoplasmic proteinsAlpha IIbCytoskeletal proteinsCanonical recognition sequenceInteracting residues
2002
The Phosphotyrosine Binding-like Domain of Talin Activates Integrins*
Calderwood DA, Yan B, de Pereda JM, Alvarez B, Fujioka Y, Liddington RC, Ginsberg MH. The Phosphotyrosine Binding-like Domain of Talin Activates Integrins*. Journal Of Biological Chemistry 2002, 277: 21749-21758. PMID: 11932255, DOI: 10.1074/jbc.m111996200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsCell AdhesionCell SeparationCHO CellsCricetinaeCytoplasmDNA, ComplementaryFlow CytometryIntegrinsKineticsLigandsModels, MolecularMolecular Sequence DataMutationPhosphotyrosineProtein BindingProtein FoldingProtein Structure, TertiaryRecombinant Fusion ProteinsRecombinant ProteinsSequence Homology, Amino AcidSurface Plasmon ResonanceTalinTime FactorsConceptsIntegrin beta cytoplasmic domainsBeta cytoplasmic domainsIntegrin beta tailsPTB domainCytoplasmic domainBeta tailsHead domainBeta3 tailPhosphotyrosine-binding (PTB) domainIntegrin adhesion receptorsBeta turnActivation of integrinsBinding-like domainsNPXY motifFERM domainTalin fragmentCellular regulationF3 subdomainsActivates IntegrinPeptide ligandsIntegrin activationAdhesion receptorsTalinMotifIntegrins
2001
PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase
Formstecher E, Ramos J, Fauquet M, Calderwood D, Hsieh J, Canton B, Nguyen X, Barnier J, Camonis J, Ginsberg M, Chneiweiss H. PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase. Developmental Cell 2001, 1: 239-250. PMID: 11702783, DOI: 10.1016/s1534-5807(01)00035-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActive Transport, Cell NucleusAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsBlotting, NorthernCell DivisionCell NucleusCell SurvivalCHO CellsCricetinaeCytoplasmDNA, ComplementaryDose-Response Relationship, DrugGreen Fluorescent ProteinsImmunohistochemistryLuminescent ProteinsMAP Kinase Signaling SystemMiceMicroscopy, FluorescenceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesModels, BiologicalMolecular Sequence DataMutationPhosphoproteinsPrecipitin TestsProtein BindingSequence Homology, Amino AcidTime FactorsTranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsERK MAP kinasePEA-15MAP kinaseERK nuclear localizationNuclear export sequenceERK-dependent transcriptionMAP kinase pathwayMultiple cell typesERK 1/2 MAP kinase pathwayExport sequenceSubcellular localizationNuclear localizationCytoplasmic sequestrationKinase pathwayIntegrin functionCell typesCell growthKinaseBiological outcomesCell proliferationGenetic deletionTranscriptionERKLocalizationProliferation