2024
Conformational response of αIIbβ3 and αVβ3 integrins to force
Kolasangiani R, Farzanian K, Chen Y, Schwartz M, Bidone T. Conformational response of αIIbβ3 and αVβ3 integrins to force. Structure 2024, 33: 289-299.e4. PMID: 39706199, DOI: 10.1016/j.str.2024.11.016.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesHumansIntegrin alphaVbeta3Mechanotransduction, CellularModels, MolecularMolecular Dynamics SimulationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein ConformationConceptsBind similar ligandsExtended conformationAvb3 integrinCellular mechanosensingAdhesion receptorsSubunit domainsCell mechanosensingPlasma membraneIntegrinMechanical signalsAll-atom simulationsSingle molecule measurementsConformational responseSubunitMechanosensingStructural dynamicsSolid tissuesCellsMolecule measurementsConformationAvb3Circulating plateletsEquivalent levelMembrane
2022
Integrin αIIbβ3 intermediates: From molecular dynamics to adhesion assembly
Tong D, Soley N, Kolasangiani R, Schwartz M, Bidone T. Integrin αIIbβ3 intermediates: From molecular dynamics to adhesion assembly. Biophysical Journal 2022, 122: 533-543. PMID: 36566352, PMCID: PMC9941721, DOI: 10.1016/j.bpj.2022.12.032.Peer-Reviewed Original ResearchBlood PlateletsLigandsMolecular Dynamics SimulationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein ConformationProtein Structure, Secondary
2000
The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*
Obergfell A, Judd B, del Pozo M, Schwartz M, Koretzky G, Shattil S. The Molecular Adapter SLP-76 Relays Signals from Platelet Integrin αIIbβ3 to the Actin Cytoskeleton*. Journal Of Biological Chemistry 2000, 276: 5916-5923. PMID: 11113155, DOI: 10.1074/jbc.m010639200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAdaptor Proteins, Signal TransducingAnimalsBlood PlateletsCell AdhesionCell Cycle ProteinsCHO CellsCricetinaeCytoskeletonEnzyme PrecursorsFibrinogenHumansIntracellular Signaling Peptides and ProteinsPhosphoproteinsPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein BindingProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-vavPseudopodiarac GTP-Binding ProteinsSignal TransductionSyk KinaseConceptsSLP-76SLAP-130Lamellipodia formationSLP-76 functionAdhesion-dependent activationCHO cell adhesionCell expression systemSLP-76 phosphorylationChinese hamster ovary cell expression systemSLP-76 expressionSyk tyrosine kinasePlatelet integrin αIIbβ3Sites of adhesionRac effectorPAK kinasesActin cytoskeletonAdherent CHO cellsExchange factorActin rearrangementCytoskeletal reorganizationActin reorganizationTyrosine phosphorylationExpression systemCell spreadingTyrosine kinase
1997
Affinity Modulation of Platelet Integrin αIIbβ3 by β3-Endonexin, a Selective Binding Partner of the β3 Integrin Cytoplasmic Tail
Kashiwagi H, Schwartz M, Eigenthaler M, Davis K, Ginsberg M, Shattil S. Affinity Modulation of Platelet Integrin αIIbβ3 by β3-Endonexin, a Selective Binding Partner of the β3 Integrin Cytoplasmic Tail. Journal Of Cell Biology 1997, 137: 1433-1443. PMID: 9182673, PMCID: PMC2132534, DOI: 10.1083/jcb.137.6.1433.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBlood PlateletsCHO CellsCricetinaeCytoplasmGene ExpressionIntegrin beta3Nuclear ProteinsPlatelet Glycoprotein GPIIb-IIIa ComplexPlatelet Membrane GlycoproteinsProteinsRecombinant Fusion ProteinsSubcellular FractionsConceptsGreen fluorescent proteinIntegrin cytoplasmic tailsCytoplasmic tailSuch protein-protein interactionsSelective binding partnerΒ3 integrin cytoplasmic tailProtein-protein interactionsAffinity modulationFibrinogen-dependent aggregationPlatelet integrin αIIbβ3Β3-endonexinBinding partnerEnergy-dependent fashionAcid proteinH-RasIntegrin alphaIIbbeta3Adhesive functionMetabolic regulationFluorescent proteinBeta3 tailIntegrin αIIbβ3Cell lysatesCHO cellsAffinity stateSurface expression
1995
Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK
Leong L, Hughes P, Schwartz M, Ginsberg M, Shattil S. Integrin signaling: roles for the cytoplasmic tails of αIIbβ3 in the tyrosine phosphorylation of pp125FAK. Journal Of Cell Science 1995, 108: 3817-3825. PMID: 8719888, DOI: 10.1242/jcs.108.12.3817.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell Adhesion MoleculesCHO CellsCricetinaeCytoplasmEnzyme ActivationFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMolecular Sequence DataMutagenesisPhosphorylationPlatelet Glycoprotein GPIIb-IIIa ComplexProtein-Tyrosine KinasesSignal TransductionConceptsAlpha IIbCytoplasmic tailTruncation mutantsFAK phosphorylationCytoplasmic tail truncation mutantsMembrane-proximal portionProtein tyrosine kinasesMembrane-distal portionExtent of phosphorylationLatter mutantTyrosine phosphorylationPersistent phosphorylationCell spreadingMutantsTyrosine kinaseCellular responsesExtracellular portionPhosphorylationCell adhesionFAKAdhesive ligandsCHO cellsPp125FAKAdditional mutationsBeta 3
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