2023
Use of Ecto-Tagged Integrins to Monitor Integrin Exocytosis and Endocytosis
Huet-Calderwood C, Rivera-Molina F, Toomre D, Calderwood D. Use of Ecto-Tagged Integrins to Monitor Integrin Exocytosis and Endocytosis. Methods In Molecular Biology 2023, 2608: 17-38. PMID: 36653699, PMCID: PMC9999384, DOI: 10.1007/978-1-0716-2887-4_2.ChaptersConceptsΒ1 integrinTotal internal reflection fluorescence microscopyNormal cell adhesionIntegrin adhesion receptorsReflection fluorescence microscopyAdhesion receptorsCell adhesionEndocytosisFluorescence microscopyExocytosisIntegrinsCellsHaloTagPHluorinIntracellular labelingEctoPhotobleachingTagsReceptorsChaseFluorescentAdhesionLabelingMigration
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
2017
Novel ecto-tagged integrins reveal their trafficking in live cells
Huet-Calderwood C, Rivera-Molina F, Iwamoto DV, Kromann EB, Toomre D, Calderwood DA. Novel ecto-tagged integrins reveal their trafficking in live cells. Nature Communications 2017, 8: 570. PMID: 28924207, PMCID: PMC5603536, DOI: 10.1038/s41467-017-00646-w.Peer-Reviewed Original ResearchConceptsIntegrin functionΒ1 integrinLive cellsCell surface adhesion receptorsHeterodimeric cell-surface adhesion receptorsIntegrin endocytosisMulticellular organismsNovel powerful toolFocal adhesionsKnockout fibroblastsIntegrin activationAdhesion receptorsExtracellular loopIntegrinsTraffickingMajor mysteriesCellsTagsAdhesionHaloTagEndocytosisPowerful toolExocytosisOrganismsVesicles
2015
Regulation of integrin-mediated adhesions
Iwamoto DV, Calderwood DA. Regulation of integrin-mediated adhesions. Current Opinion In Cell Biology 2015, 36: 41-47. PMID: 26189062, PMCID: PMC4639423, DOI: 10.1016/j.ceb.2015.06.009.Peer-Reviewed Original ResearchConceptsIntegrin-mediated adhesionHeterodimeric transmembrane adhesion receptorsShort cytoplasmic tailTransmembrane adhesion receptorsSpecific intracellular proteinsClustering of integrinsMetazoan developmentActin cytoskeletonExtracellular ligandsCytoplasmic tailIntracellular traffickingExtracellular environmentIntracellular proteinsAdhesion receptorsAdhesive structuresIntegrin receptorsCell membraneRelay signalsIntegrinsEssential roleMechanical forcesCell attachmentAdhesionRecent advancesCytoskeleton
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 levelSignalingIntegrin Cytoplasmic Tail Interactions
Morse EM, Brahme NN, Calderwood DA. Integrin Cytoplasmic Tail Interactions. Biochemistry 2014, 53: 810-820. PMID: 24467163, PMCID: PMC3985435, DOI: 10.1021/bi401596q.Peer-Reviewed Original ResearchConceptsIntegrin-interacting proteinsIntegrin cytoplasmic tailsCell surface adhesion receptorsIntegrin-binding proteinsHeterodimeric cell-surface adhesion receptorsSurface adhesion receptorsExtracellular ligandsMulticellular lifeCytoplasmic tailIntegrin engagementCell motilityExtracellular environmentTransduce chemicalIntegrin activityIntegrin localizationIntracellular proteinsAdhesion receptorsTail interactionsMechanical signalsProteinIntegrinsCellsCytoskeletonLocalizationTrafficking
2012
Zasp regulates integrin activation
Bouaouina M, Jani K, Long JY, Czerniecki S, Morse EM, Ellis SJ, Tanentzapf G, Schöck F, Calderwood DA. Zasp regulates integrin activation. Journal Of Cell Science 2012, 125: 5647-5657. PMID: 22992465, PMCID: PMC3575701, DOI: 10.1242/jcs.103291.Peer-Reviewed Original ResearchConceptsIntegrin activationDomain-containing proteinsExtracellular matrixHeterodimeric adhesion receptorsPDZ motif-containing proteinΑ5β1 integrinMammalian tissue cultureScaffold proteinCytoplasmic tailFirst proteinECM ligandsMuscle contractile machineryΒ-integrinExtracellular domainAdhesion receptorsIntegrin heterodimersTalinConformational changesHigh-affinity bindingEssential processProteinIntegrinsHuman cardiomyopathyZASPTissue cultureCell Adhesion: A FERM Grasp of the Tail Sorts Out Integrins
Brahme NN, Calderwood DA. Cell Adhesion: A FERM Grasp of the Tail Sorts Out Integrins. Current Biology 2012, 22: r692-r694. PMID: 22974999, PMCID: PMC5507346, DOI: 10.1016/j.cub.2012.07.049.Peer-Reviewed Original ResearchFunctional differences between kindlin-1 and kindlin-2 in keratinocytes
Bandyopadhyay A, Rothschild G, Kim S, Calderwood DA, Raghavan S. Functional differences between kindlin-1 and kindlin-2 in keratinocytes. Journal Of Cell Science 2012, 125: 2172-2184. PMID: 22328497, PMCID: PMC3367939, DOI: 10.1242/jcs.096214.Peer-Reviewed Original ResearchConceptsFocal adhesionsKindlin-2Kindlin-1Cell spreadingPeripheral focal adhesionsIntegrin β1Wild-type cellsUnexpected functional consequencesIntegrin β6Wild-type keratinocytesCytoplasmic tailNull keratinocytesKindlinNull cellsFunctional consequencesDirect interactionFunctional differencesUnique functionRelated integrinsIntegrinsCellsAdhesionKeratinocytesIntegrin αvβ6Knockdown
2011
Talin and Signaling Through Integrins
Bouaouina M, Harburger DS, Calderwood DA. Talin and Signaling Through Integrins. Methods In Molecular Biology 2011, 757: 325-347. PMID: 21909921, PMCID: PMC5642996, DOI: 10.1007/978-1-61779-166-6_20.Peer-Reviewed Original ResearchConceptsCytoplasmic tailIntegrin activationIntegrin β tailsAbility of integrinsIntegrin cytoplasmic tailsShort cytoplasmic tailIntegrin adhesion receptorsBinding of talinDominant-negative constructMulticellular animalsActin cytoskeletonΒ tailExtracellular ligandsTalin domainTalinCharacterization of interactionsIntracellular signalsAdhesion receptorsCell adhesionIntegrin receptorsCultured cellsExtracellular matrixNegative constructsIntegrin subunitsIntegrins
2009
Filamin A–β1 Integrin Complex Tunes Epithelial Cell Response to Matrix Tension
Gehler S, Baldassarre M, Lad Y, Leight JL, Wozniak MA, Riching KM, Eliceiri KW, Weaver VM, Calderwood DA, Keely PJ. Filamin A–β1 Integrin Complex Tunes Epithelial Cell Response to Matrix Tension. Molecular Biology Of The Cell 2009, 20: 3224-3238. PMID: 19458194, PMCID: PMC2710838, DOI: 10.1091/mbc.e08-12-1186.Peer-Reviewed Original ResearchConceptsFilamin AExtracellular matrixProtein filamin AHigh-density gelsMatrix tensionCollagen gelsMechanosensitive complexBreast epithelial cellsCellular contractilityMatrix stiffnessMorphogenesisEpithelial cell responsesCell typesDuctal morphogenesisEpithelial cellsCellsCollagen matrixGel contractionActinCollagen remodelingIntegrinsCell responsesCollagen fibrilsRemodelingGel
2007
The N-terminal Domains of Talin Cooperate with the Phosphotyrosine Binding-like Domain to Activate β1 and β3 Integrins*
Bouaouina M, Lad Y, Calderwood DA. The N-terminal Domains of Talin Cooperate with the Phosphotyrosine Binding-like Domain to Activate β1 and β3 Integrins*. Journal Of Biological Chemistry 2007, 283: 6118-6125. PMID: 18165225, DOI: 10.1074/jbc.m709527200.Peer-Reviewed Original Research
2006
Integrins in the Ovary
Monniaux D, Huet-Calderwood C, Bellego F, Fabre S, Monget P, Calderwood D. Integrins in the Ovary. Seminars In Reproductive Medicine 2006, 24: 251-261. PMID: 16944422, DOI: 10.1055/s-2006-948554.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsRole of integrinsSperm ADAMsActin cytoskeletonExtracellular matrix componentsIntegrin tailsMultiple signalingOocyte integrinsOvarian surface epithelium cellsIntegrin functionConformational changesExtracellular matrixIntegrinsCell proliferationMatrix componentsTumor developmentMajor receptorIntegrin expressionSurface epithelium cellsPossible involvementPotential roleFollicular cellsGranulosa cellsCellsFollicular basement membraneEpithelium cells
2004
Competition for Talin Results in Trans-dominant Inhibition of Integrin Activation*
Calderwood DA, Tai V, Di Paolo G, De Camilli P, Ginsberg MH. Competition for Talin Results in Trans-dominant Inhibition of Integrin Activation*. Journal Of Biological Chemistry 2004, 279: 28889-28895. PMID: 15143061, DOI: 10.1074/jbc.m402161200.Peer-Reviewed Original ResearchConceptsTrans-dominant inhibitionIntegrin activationFragment of talinCytoskeletal protein talinIntegrin adhesion receptorsMulticellular animalsProtein talinExtracellular ligandsCellular processesBeta tailsTalinTransdominant inhibitionAdhesion receptorsDifferent integrinsOverexpression of integrinsIntegrinsActivationClot retractionInhibitionReceptorsTailAdhesionSpeciesProteinOverexpression
2003
Talin forges the links between integrins and actin
Calderwood DA, Ginsberg MH. Talin forges the links between integrins and actin. Nature Cell Biology 2003, 5: 694-696. PMID: 12894175, DOI: 10.1038/ncb0803-694.Peer-Reviewed Original Research
2002
The 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
2000
Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport*
Fenczik C, Zent R, Dellos M, Calderwood D, Satriano J, Kelly C, Ginsberg M. Distinct Domains of CD98hc Regulate Integrins and Amino Acid Transport*. Journal Of Biological Chemistry 2000, 276: 8746-8752. PMID: 11121428, DOI: 10.1074/jbc.m011239200.Peer-Reviewed Original ResearchConceptsAmino acid transportIntegrin functionAcid transportDistinct domainsType II transmembrane proteinIsoleucine transportAmino acid transportersCD98 heavy chainCell surface heterodimersTransmembrane domainCytoplasmic domainTransmembrane proteinSurface heterodimersExtracellular domainAcid transportersCD98hcHeavy chainProteinIntegrinsCovalent linkageDifferent light chainsLight chainDomainMutantsHeterodimersIntegrin cytoplasmic domain-binding proteins
Liu S, Calderwood D, Ginsberg M. Integrin cytoplasmic domain-binding proteins. Journal Of Cell Science 2000, 113: 3563-3571. PMID: 11017872, DOI: 10.1242/jcs.113.20.3563.Peer-Reviewed Original ResearchConceptsDomain-binding proteinCytoplasmic domainCellular proteinsIntegrin cytoplasmic domainActin-binding proteinsMore cellular proteinsCell surface receptorsGene regulationCellular functionsTransduce signalsSignal transductionBiological functionsGene expressionFunctional analysisCell adhesionLarge familySurface receptorsProteinCytoskeletonIntegrin chainsIntegrinsBiological responsesPivotal roleMechanical linkImportant roleClass- 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