2022
Organization, dynamics and mechanoregulation of integrin-mediated cell–ECM adhesions
Kanchanawong P, Calderwood DA. Organization, dynamics and mechanoregulation of integrin-mediated cell–ECM adhesions. Nature Reviews Molecular Cell Biology 2022, 24: 142-161. PMID: 36168065, PMCID: PMC9892292, DOI: 10.1038/s41580-022-00531-5.Peer-Reviewed Original ResearchConceptsExtracellular matrixCell-ECM adhesionCell-ECM interactionsLocal extracellular matrixAdhesion maturationAdhesion complexesAnimal cellsBiochemical signalingTransmembrane receptorsAdhesion structuresCell shapeIntegrin familyMolecular natureAge-related dysfunctionAdvanced imaging approachesCharacterization of rearrangementsMechanical forcesSignalingTissue formationAdhesionCytoskeletonMechanoregulationImmune responseImaging approachImproved understanding
2020
Chapter 22: Structural and signaling functions of integrins
Kadry YA, Calderwood DA. Chapter 22: Structural and signaling functions of integrins. Biochimica Et Biophysica Acta (BBA) - Biomembranes 2020, 1862: 183206. PMID: 31991120, PMCID: PMC7063833, DOI: 10.1016/j.bbamem.2020.183206.Peer-Reviewed Original ResearchConceptsFunction of integrinsAbility of integrinsTransmembrane adhesion receptorsNon-redundant functionsDifferent integrin heterodimersExtracellular matrix proteinsComplex structural rearrangementsDiverse downstreamCytoskeletal complexMetazoan lifeExtracellular environmentΒ-subunitAdhesion receptorsIntegrin heterodimersIntegrin familyMatrix proteinsCell adhesionIntegrinsStructural rearrangementsHeterodimersRecent advancesSubunitsSignalingProteinFunction
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
Dynamin 2 regulation of integrin endocytosis, but not VEGF signaling, is crucial for developmental angiogenesis
Lee MY, Skoura A, Park EJ, Landskroner-Eiger S, Jozsef L, Luciano AK, Murata T, Pasula S, Dong Y, Bouaouina M, Calderwood DA, Ferguson SM, De Camilli P, Sessa WC. Dynamin 2 regulation of integrin endocytosis, but not VEGF signaling, is crucial for developmental angiogenesis. Development 2014, 141: 1465-1472. PMID: 24598168, PMCID: PMC3957370, DOI: 10.1242/dev.104539.Peer-Reviewed Original ResearchConceptsΒ1 integrinFocal adhesion sizeGrowth factor signalingVascular endothelial growth factor signalingEndocytic turnoverIntegrin endocytosisDynamin 2Adhesion sizeFactor signalingDevelopmental angiogenesisAngiogenic sproutingCell migrationCultured endothelial cellsMultiple integrinsInducible lossIntegrinsMorphogenesisActivation stateDNM2Endothelial cellsAngiogenesisVivoEndocytosisSurface levelSignalingDifferences 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
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