2018
Kindlin-2 interacts with a highly conserved surface of ILK to regulate focal adhesion localization and cell spreading
Kadry YA, Huet-Calderwood C, Simon B, Calderwood DA. Kindlin-2 interacts with a highly conserved surface of ILK to regulate focal adhesion localization and cell spreading. Journal Of Cell Science 2018, 131: jcs221184. PMID: 30254023, PMCID: PMC6215391, DOI: 10.1242/jcs.221184.Peer-Reviewed Original ResearchConceptsIntegrin-linked kinaseFocal adhesion localizationKindlin-2Cell spreadingIntegrin-mediated signalingILK bindingILK mutantPseudokinase domainIntegrin signalingKnockdown cellsAxis downstreamC-lobeCell morphologyMutantsSignalingCentral rolePKDComplete understandingLocalizationFirst personKinaseAdaptorSitesSpeciesIntegrins
2014
Differences in binding to the ILK complex determines kindlin isoform adhesion localization and integrin activation
Huet-Calderwood C, Brahme NN, Kumar N, Stiegler AL, Raghavan S, Boggon TJ, Calderwood DA. Differences in binding to the ILK complex determines kindlin isoform adhesion localization and integrin activation. Journal Of Cell Science 2014, 127: 4308-4321. PMID: 25086068, PMCID: PMC4179494, DOI: 10.1242/jcs.155879.Peer-Reviewed Original ResearchConceptsIntegrin activationKindlin-2Kindlin-3Focal adhesion proteinsFunctional differencesIntegrin-linked kinaseILK complexAdhesion proteinsF2 subdomainMolecular basisIsoform specificityComplex bindsKindlinFA targetingActivation defectsCell adhesionActivationFALocalizesKinaseGFPSignalingILKIsoformsProtein
2012
Structural Basis for Paxillin Binding and Focal Adhesion Targeting of β-Parvin*
Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, Boggon TJ. Structural Basis for Paxillin Binding and Focal Adhesion Targeting of β-Parvin*. Journal Of Biological Chemistry 2012, 287: 32566-32577. PMID: 22869380, PMCID: PMC3463362, DOI: 10.1074/jbc.m112.367342.Peer-Reviewed Original ResearchConceptsΒ-parvinFocal adhesionsPaxillin bindingΑ-parvinFocal adhesion targetingN-terminal α-helixPaxillin LD1 motifCalponin homology domainFirst molecular detailsHigh sequence similarityCytoplasmic adaptor proteinIntegrin-linked kinasePaxillin LD1Co-crystal structureLD4 motifSignificant conformational flexibilityHomology domainAdaptor proteinCellular functionsSequence similarityRepeat motifsProper localizationMolecular detailsPaxillinStructural basis
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 sitesKinaseDomainAnkyrinParvinMutagenesisMammals
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