2021
A Small-Scale shRNA Screen in Primary Mouse Macrophages Identifies a Role for the Rab GTPase Rab1b in Controlling Salmonella Typhi Growth
Solano-Collado V, Colamarino RA, Calderwood DA, Baldassarre M, Spanò S. A Small-Scale shRNA Screen in Primary Mouse Macrophages Identifies a Role for the Rab GTPase Rab1b in Controlling Salmonella Typhi Growth. Frontiers In Cellular And Infection Microbiology 2021, 11: 660689. PMID: 33898333, PMCID: PMC8059790, DOI: 10.3389/fcimb.2021.660689.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsMacrophagesMiceRab GTP-Binding ProteinsRNA, Small InterferingSalmonella typhiTyphoid FeverConceptsShRNA screenMouse macrophagesGenome-wide screeningRab GTPasesRab GTPasePrimary mouse macrophagesGTPase Rab1bNext-generation sequencingLife-threatening systemic infectionsUnbiased identificationFluorescent populationsConcept screenIntracellular pathogensPrimary immune cellsRab32Bacterial pathogensRab1bHuman hostPrimary mouseInfected cellsHuman macrophagesImportance of macrophagesSalmonella typhi growthTyphi infectionImmune cellsPPP6C negatively regulates oncogenic ERK signaling through dephosphorylation of MEK
Cho E, Lou HJ, Kuruvilla L, Calderwood DA, Turk BE. PPP6C negatively regulates oncogenic ERK signaling through dephosphorylation of MEK. Cell Reports 2021, 34: 108928. PMID: 33789117, PMCID: PMC8068315, DOI: 10.1016/j.celrep.2021.108928.Peer-Reviewed Original ResearchConceptsProtein kinase cascadeCore oncogenic pathwaysKey negative regulatorOncogenic ERKERK pathway activationCrosstalk regulationCentral kinaseKinase cascadePhosphorylation sitesRegulatory subunitRaf-MEKNegative regulatorERK pathwayDrug targetsOncogenic pathwaysMEKMEK inhibitorsDephosphorylationPathway activationPPP6CPhosphatasePathwayERKHyperphosphorylationCascade
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
2014
Up-regulation of Thrombospondin-2 in Akt1-null Mice Contributes to Compromised Tissue Repair Due to Abnormalities in Fibroblast Function*
Bancroft T, Bouaouina M, Roberts S, Lee M, Calderwood DA, Schwartz M, Simons M, Sessa WC, Kyriakides TR. Up-regulation of Thrombospondin-2 in Akt1-null Mice Contributes to Compromised Tissue Repair Due to Abnormalities in Fibroblast Function*. Journal Of Biological Chemistry 2014, 290: 409-422. PMID: 25389299, PMCID: PMC4281743, DOI: 10.1074/jbc.m114.618421.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MovementFibroblastsGene Expression RegulationGenetic Complementation TestIntegrin beta1MiceMice, KnockoutNeuropeptidesNitric Oxide Synthase Type IIIPrimary Cell CultureProto-Oncogene Proteins c-aktRac1 GTP-Binding ProteinRNA, Small InterferingSignal TransductionSkinThrombospondinsWound HealingWounds, Nonpenetrating
2012
Macrophage Mesenchymal Migration Requires Podosome Stabilization by Filamin A*
Guiet R, Vérollet C, Lamsoul I, Cougoule C, Poincloux R, Labrousse A, Calderwood DA, Glogauer M, Lutz PG, Maridonneau-Parini I. Macrophage Mesenchymal Migration Requires Podosome Stabilization by Filamin A*. Journal Of Biological Chemistry 2012, 287: 13051-13062. PMID: 22334688, PMCID: PMC3339984, DOI: 10.1074/jbc.m111.307124.Peer-Reviewed Original ResearchConceptsFilamin AMesenchymal migrationEmbryonic developmentPodosome rosette formationCell migrationMesenchymal migration modeCertain cell typesPodosome stabilityScaffold proteinActin polymerizationAmoeboid migrationNull mutationPodosomesActin filamentsMigratory cellsAmoeboid modeCell typesOrgan defectsMigration modesNew functionsThree-dimensional environmentMutationsProteaseStrong consequencesFLNA mutations
2008
ASB2 targets filamins A and B to proteasomal degradation
Heuzé ML, Lamsoul I, Baldassarre M, Lad Y, Lévêque S, Razinia Z, Moog-Lutz C, Calderwood DA, Lutz PG. ASB2 targets filamins A and B to proteasomal degradation. Blood 2008, 112: 5130-5140. PMID: 18799729, PMCID: PMC2597609, DOI: 10.1182/blood-2007-12-128744.Peer-Reviewed Original ResearchConceptsAnkyrin repeat-containing proteinFilamin AE3 ubiquitin ligase complexActin-binding protein filamin AFilamin degradationRepeat-containing proteinUbiquitin ligase complexSeries of proliferationHematopoietic cell differentiationProtein filamin AAcid-induced differentiationSuppressor of cytokineLigase complexSpecificity subunitLeukemia cellsHematopoietic differentiationHematopoietic progenitor cellsProteasomal degradationMolecular basisAcute promyelocytic leukemia cellsSpecific proteinsCell spreadingPromyelocytic leukemia cellsArrest of differentiationCell differentiation
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