2020
Serine phosphorylation of the small phosphoprotein ICAP1 inhibits its nuclear accumulation
Su VL, Simon B, Draheim KM, Calderwood DA. Serine phosphorylation of the small phosphoprotein ICAP1 inhibits its nuclear accumulation. Journal Of Biological Chemistry 2020, 295: 3269-3284. PMID: 32005669, PMCID: PMC7062153, DOI: 10.1074/jbc.ra119.009794.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCatalytic DomainCell NucleusCHO CellsCricetinaeCricetulusHumansKRIT1 ProteinMutagenesis, Site-DirectedP21-Activated KinasesPhosphorylationSerineConceptsIntegrin cytoplasmic domain-associated protein-1N-terminal regionNuclear accumulationP21-activated kinase 4Ser-10Nuclear roleSerine phosphorylationNuclear localizationPhosphorylation-mimicking substitutionsNuclear localization signalCell-cell junctionsSer-25Localization signalKRIT1 functionThreonine residuesAdaptor proteinKRIT1 lossSubcellular localizationNeurovascular dysplasiaBlood vessel integrityVascular developmentKinase 4Cultured cellsPhosphorylationProtein 1
2016
Nuclear Localization of Integrin Cytoplasmic Domain-associated Protein-1 (ICAP1) Influences β1 Integrin Activation and Recruits Krev/Interaction Trapped-1 (KRIT1) to the Nucleus*
Draheim KM, Huet-Calderwood C, Simon B, Calderwood DA. Nuclear Localization of Integrin Cytoplasmic Domain-associated Protein-1 (ICAP1) Influences β1 Integrin Activation and Recruits Krev/Interaction Trapped-1 (KRIT1) to the Nucleus*. Journal Of Biological Chemistry 2016, 292: 1884-1898. PMID: 28003363, PMCID: PMC5290960, DOI: 10.1074/jbc.m116.762393.Peer-Reviewed Original Research
2015
The Rap1-RIAM pathway prefers β2 integrins
Calderwood DA. The Rap1-RIAM pathway prefers β2 integrins. Blood 2015, 126: 2658-2659. PMID: 26679542, PMCID: PMC4683328, DOI: 10.1182/blood-2015-09-668962.Peer-Reviewed Original ResearchAdaptor Proteins, Signal TransducingAnimalsB-LymphocytesCD18 AntigensChemotaxis, LeukocyteLeukocytesMembrane ProteinsT-Lymphocytes
2013
Purification and SAXS Analysis of the Integrin Linked Kinase, PINCH, Parvin (IPP) Heterotrimeric Complex
Stiegler AL, Grant TD, Luft JR, Calderwood DA, Snell EH, Boggon TJ. Purification and SAXS Analysis of the Integrin Linked Kinase, PINCH, Parvin (IPP) Heterotrimeric Complex. PLOS ONE 2013, 8: e55591. PMID: 23383235, PMCID: PMC3561323, DOI: 10.1371/journal.pone.0055591.Peer-Reviewed Original ResearchConceptsIPP complexEnsemble optimization methodDetailed purification protocolHeterotrimeric protein complexIntegrin Linked KinaseIntegrin adhesion receptorsInter-domain linkerInter-domain interactionsInter-domain contactsGel filtration analysisΑ-parvinLIM1 domainHuman ILKSmall-angle X-ray scatteringHeterotrimeric complexProtein complexesFocal adhesionsAdhesion receptorsPINCH proteinFirst structural characterizationFiltration analysisPurification protocolConformational restraintsKinaseILKMechanism for KRIT1 Release of ICAP1-Mediated Suppression of Integrin Activation
Liu W, Draheim KM, Zhang R, Calderwood DA, Boggon TJ. Mechanism for KRIT1 Release of ICAP1-Mediated Suppression of Integrin Activation. Molecular Cell 2013, 49: 719-729. PMID: 23317506, PMCID: PMC3684052, DOI: 10.1016/j.molcel.2012.12.005.Peer-Reviewed Original ResearchAdaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceCell Line, TumorConserved SequenceCrystallography, X-RayHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsIntegrin beta1Intracellular Signaling Peptides and ProteinsKRIT1 ProteinMembrane ProteinsMicrotubule-Associated ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternaryProto-Oncogene ProteinsSignal Transduction
2011
Functional and Structural Insights into ASB2α, a Novel Regulator of Integrin-dependent Adhesion of Hematopoietic Cells*
Lamsoul I, Burande CF, Razinia Z, Houles TC, Menoret D, Baldassarre M, Erard M, Moog-Lutz C, Calderwood DA, Lutz PG. Functional and Structural Insights into ASB2α, a Novel Regulator of Integrin-dependent Adhesion of Hematopoietic Cells*. Journal Of Biological Chemistry 2011, 286: 30571-30581. PMID: 21737450, PMCID: PMC3162417, DOI: 10.1074/jbc.m111.220921.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsCarrier ProteinsCell AdhesionFibronectinsGene Expression RegulationHeLa CellsHematopoietic Stem CellsHumansIntegrinsMiceMusclesNIH 3T3 CellsProtein BindingProtein Structure, TertiarySubstrate SpecificitySuppressor of Cytokine Signaling ProteinsConceptsN-terminal regionHematopoietic cellsE3 ubiquitin ligase complexE3 ubiquitin ligase functionShort N-terminal regionUbiquitin ligase complexUbiquitin ligase functionAcid-responsive genesIntegrin-dependent adhesionRetinoic acid-responsive geneCell fateLigase complexSpecificity subunitLigase functionResponsive genesLeukemia cellsProteasomal degradationNovel regulatorFilamin A.Myogenic differentiationStructural insightsASB2αΒ-integrinAcute promyelocytic leukemia cellsStructural homology
2009
Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase
Chiswell BP, Stiegler AL, Razinia Z, Nalibotski E, Boggon TJ, Calderwood DA. Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. Journal Of Structural Biology 2009, 170: 157-163. PMID: 19963065, PMCID: PMC2841223, DOI: 10.1016/j.jsb.2009.12.002.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnkyrin RepeatBinding, CompetitiveCrystallizationDNA-Binding ProteinsGene Expression RegulationLIM Domain ProteinsMembrane ProteinsModels, MolecularMolecular Sequence DataMutagenesisProtein BindingProtein Serine-Threonine KinasesSignal TransductionConceptsIntegrin-linked kinaseAnkyrin repeat domainLIM1 domainIPP complexIsoform-specific functionsIntegrin adhesion receptorsDifferent cellular responsesPINCH2Repeat domainPINCH1Point mutagenesisStructural basisAdhesion receptorsCellular responsesAlters localizationDifferential regulationSame binding siteDirect competitionBinding sitesKinaseDomainAnkyrinParvinMutagenesisMammalsThe 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
2008
The structural basis of integrin-linked kinase–PINCH interactions
Chiswell BP, Zhang R, Murphy JW, Boggon TJ, Calderwood DA. The structural basis of integrin-linked kinase–PINCH interactions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 20677-20682. PMID: 19074270, PMCID: PMC2634877, DOI: 10.1073/pnas.0811415106.Peer-Reviewed Original ResearchConceptsIntegrin-linked kinaseLIM1 domainGrowth factor signalingAtomic resolution descriptionILK bindingAnkyrin repeatsILK-PINCHHeterotrimeric complexZinc fingerMolecular basisMutagenesis dataStructural basisCell adhesionPoint mutationsConformational flexibilityKey interactionsParvinConvergence pointLim1DomainAnkyrinKinaseComplexesRepeatsSignaling