2013
Substrate and Inhibitor Specificity of the Type II p21-Activated Kinase, PAK6
Gao J, Ha BH, Lou HJ, Morse EM, Zhang R, Calderwood DA, Turk BE, Boggon TJ. Substrate and Inhibitor Specificity of the Type II p21-Activated Kinase, PAK6. PLOS ONE 2013, 8: e77818. PMID: 24204982, PMCID: PMC3810134, DOI: 10.1371/journal.pone.0077818.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCatalytic DomainCrystallizationCrystallography, X-RayHEK293 CellsHumansIndolesModels, MolecularMolecular Sequence DataP21-Activated KinasesPeptide FragmentsPhosphorylationProtein ConformationPyrazolesPyrrolesSequence Homology, Amino AcidSignal TransductionSubstrate SpecificitySunitinibConceptsP21-activated kinaseCo-crystal structureRho family small GTPasesPeptide substrate specificityATP-competitive inhibitorsStructure-function relationshipsSmall GTPasesPAK familyCatalytic domainMelanoma-associated mutationsSubstrate specificityInhibitor specificityPAK6Receptor signalingPF-3758309Important effectors
2012
Structural Basis for Small G Protein Effector Interaction of Ras-related Protein 1 (Rap1) and Adaptor Protein Krev Interaction Trapped 1 (KRIT1)
Li X, Zhang R, Draheim KM, Liu W, Calderwood DA, Boggon TJ. Structural Basis for Small G Protein Effector Interaction of Ras-related Protein 1 (Rap1) and Adaptor Protein Krev Interaction Trapped 1 (KRIT1). Journal Of Biological Chemistry 2012, 287: 22317-22327. PMID: 22577140, PMCID: PMC3381192, DOI: 10.1074/jbc.m112.361295.Peer-Reviewed Original ResearchAmino Acid SequenceCrystallography, X-RayGene Expression RegulationGTP PhosphohydrolasesHemangioma, Cavernous, Central Nervous SystemHumansIntegrinsKRIT1 ProteinMicrotubule-Associated ProteinsModels, BiologicalModels, MolecularMolecular Sequence DataMutagenesisPoint MutationProtein ConformationProtein Interaction MappingProtein Structure, TertiaryProto-Oncogene ProteinsRap1 GTP-Binding ProteinsSequence Homology, Amino AcidSignal Transduction
2009
The Structure of the N-Terminus of Kindlin-1: A Domain Important for αIIbβ3 Integrin Activation
Goult BT, Bouaouina M, Harburger DS, Bate N, Patel B, Anthis NJ, Campbell ID, Calderwood DA, Barsukov IL, Roberts GC, Critchley DR. The Structure of the N-Terminus of Kindlin-1: A Domain Important for αIIbβ3 Integrin Activation. Journal Of Molecular Biology 2009, 394: 944-956. PMID: 19804783, PMCID: PMC2963925, DOI: 10.1016/j.jmb.2009.09.061.Peer-Reviewed Original Research
2006
The Molecular Basis of Filamin Binding to Integrins and Competition with Talin
Kiema T, Lad Y, Jiang P, Oxley CL, Baldassarre M, Wegener KL, Campbell ID, Ylänne J, Calderwood DA. The Molecular Basis of Filamin Binding to Integrins and Competition with Talin. Molecular Cell 2006, 21: 337-347. PMID: 16455489, DOI: 10.1016/j.molcel.2006.01.011.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCalpainContractile ProteinsCrystallography, X-RayFilaminsIntegrin beta ChainsMiceMicrofilament ProteinsModels, MolecularMolecular Sequence DataNIH 3T3 CellsNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationProtein Structure, TertiaryRecombinant Fusion ProteinsReproducibility of ResultsSequence Homology, Amino AcidTalinConceptsAdhesion receptorsTalin-dependent integrin activationActin-crosslinking proteinsIntegrin adhesion receptorsHigh-resolution structuresFilamin bindingExtended beta strandActin cytoskeletonIntegrin tailsMultiple transmembraneMolecular basisStrands CBeta strandsDomain interactionsBiochemical signalsIntegrin functionIntegrin activationFilamin ATalinCell membraneTail formsCytoskeletonProteinBinding sitesFilamin
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 cellsIntegrin 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 N-terminal SH2 Domains of Syk and ZAP-70 Mediate Phosphotyrosine-independent Binding to Integrin β Cytoplasmic Domains*
Woodside DG, Obergfell A, Talapatra A, Calderwood DA, Shattil SJ, Ginsberg MH. The N-terminal SH2 Domains of Syk and ZAP-70 Mediate Phosphotyrosine-independent Binding to Integrin β Cytoplasmic Domains*. Journal Of Biological Chemistry 2002, 277: 39401-39408. PMID: 12171941, DOI: 10.1074/jbc.m207657200.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDose-Response Relationship, DrugEnzyme PrecursorsGenetic VectorsGlutathione TransferaseIntegrin beta ChainsIntracellular Signaling Peptides and ProteinsKineticsModels, GeneticMolecular Sequence DataNickelPhosphorylationPhosphotyrosinePrecipitin TestsProtein BindingProtein Structure, TertiaryProtein-Tyrosine KinasesRecombinant Fusion ProteinsSequence Homology, Amino AcidSrc Homology DomainsSurface Plasmon ResonanceSyk KinaseTime FactorsZAP-70 Protein-Tyrosine KinaseThe 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
2000
Class- 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
1997
Molecular Characterisation of Integrin–Procollagen C‐Propeptide Interactions
Davies D, Tuckwell DS, Calderwood DA, Weston SA, Takigawa M, Humphries MJ. Molecular Characterisation of Integrin–Procollagen C‐Propeptide Interactions. The FEBS Journal 1997, 246: 274-282. PMID: 9208915, DOI: 10.1111/j.1432-1033.1997.t01-1-00274.x.Peer-Reviewed Original Research