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
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