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
2015
Direct Interactions with the Integrin β1 Cytoplasmic Tail Activate the Abl2/Arg Kinase*
Simpson MA, Bradley WD, Harburger D, Parsons M, Calderwood DA, Koleske AJ. Direct Interactions with the Integrin β1 Cytoplasmic Tail Activate the Abl2/Arg Kinase*. Journal Of Biological Chemistry 2015, 290: 8360-8372. PMID: 25694433, PMCID: PMC4375489, DOI: 10.1074/jbc.m115.638874.Peer-Reviewed Original ResearchConceptsIntegrin β1 cytoplasmic tailExtracellular matrix adhesion receptorsSrc homology domainFibroblast cell motilityIntegrin β1Β1 cytoplasmic tailMembrane-proximal segmentAdhesion complex formationMatrix adhesion receptorsNonreceptor tyrosine kinaseArg kinase activityArg nonreceptor tyrosine kinaseCancer cell invasivenessHomology domainActin cytoskeletonCytoplasmic tailCytoskeletal remodelingDendrite morphogenesisTyr-783Kinase domainPhosphorylated regionAbl familyΒ1 tailArg kinaseCell motilityPAK6 targets to cell–cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape
Morse EM, Sun X, Olberding JR, Ha BH, Boggon TJ, Calderwood DA. PAK6 targets to cell–cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape. Journal Of Cell Science 2015, 129: 380-393. PMID: 26598554, PMCID: PMC4732285, DOI: 10.1242/jcs.177493.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, CDCadherinsCdc42 GTP-Binding ProteinCell AdhesionCell Line, TumorEpithelial CellsHEK293 CellsHumansIntercellular JunctionsMolecular Sequence DataP21-Activated KinasesProtein BindingProtein Interaction Domains and MotifsProtein Sorting SignalsProtein TransportConceptsCell-cell adhesionN-terminusCdc42/Rac interactive binding (CRIB) domainSerine/threonine kinaseP21-activated kinase (PAK) familyCdc42-dependent mannerPolybasic regionThreonine kinaseCdc42 knockdownKinase familyBinding domainsKinase activityImportant regulatorCell adhesionPAK6Broader rolePAKAdhesionTargetingCdc42PAK1KinaseKnockdownRegulatorMutations
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
2012
Nanopatterning reveals an ECM area threshold for focal adhesion assembly and force transmission that is regulated by integrin activation and cytoskeleton tension
Coyer SR, Singh A, Dumbauld DW, Calderwood DA, Craig SW, Delamarche E, García AJ. Nanopatterning reveals an ECM area threshold for focal adhesion assembly and force transmission that is regulated by integrin activation and cytoskeleton tension. Journal Of Cell Science 2012, 125: 5110-5123. PMID: 22899715, PMCID: PMC3533393, DOI: 10.1242/jcs.108035.Peer-Reviewed Original ResearchConceptsFocal adhesionsForce transductionFA assemblyCytoskeletal tensionExtracellular matrixIntegrin activationFocal adhesion assemblyVinculin head domainExpression of talinNon-migrating cellsVinculin mutantsCytoskeleton tensionAdhesion assemblyECM ligandsMyosin contractilityAdhesive areaStable assemblyIntracellular pathwaysTransductionAssemblyStructural linkPathwayStructural linkagesTraction forceCells
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