2014
TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
Uchil PD, Pawliczek T, Reynolds TD, Ding S, Hinz A, Munro JB, Huang F, Floyd RW, Yang H, Hamilton WL, Bewersdorf J, Xiong Y, Calderwood DA, Mothes W. TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly. Journal Of Cell Science 2014, 127: 3928-3942. PMID: 25015296, PMCID: PMC4163643, DOI: 10.1242/jcs.143537.Peer-Reviewed Original ResearchConceptsFocal adhesion proteinsFocal adhesionsCell migrationAdhesion proteinsMulti-adaptor proteinTripartite motif (TRIM) protein familyFocal adhesion dynamicsFocal adhesion turnoverFocal adhesion componentsCoiled-coil domainImpaired cell migrationII-independent mannerLD2 motifAdhesion turnoverActin cytoskeletonProtein familyAdhesion dynamicsCellular functionsDynamic turnoverMacromolecular complexesRegulatory componentsFocal contactsAdhesion componentsExtracellular matrixTRIM15
2002
The N-terminal SH2 Domains of Syk and ZAP-70 Mediate Phosphotyrosine-independent Binding to Integrin β Cytoplasmic Domains*
Woodside DG, Obergfell A, Talapatra A, Calderwood DA, Shattil SJ, Ginsberg MH. The N-terminal SH2 Domains of Syk and ZAP-70 Mediate Phosphotyrosine-independent Binding to Integrin β Cytoplasmic Domains*. Journal Of Biological Chemistry 2002, 277: 39401-39408. PMID: 12171941, DOI: 10.1074/jbc.m207657200.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDose-Response Relationship, DrugEnzyme PrecursorsGenetic VectorsGlutathione TransferaseIntegrin beta ChainsIntracellular Signaling Peptides and ProteinsKineticsModels, GeneticMolecular Sequence DataNickelPhosphorylationPhosphotyrosinePrecipitin TestsProtein BindingProtein Structure, TertiaryProtein-Tyrosine KinasesRecombinant Fusion ProteinsSequence Homology, Amino AcidSrc Homology DomainsSurface Plasmon ResonanceSyk KinaseTime FactorsZAP-70 Protein-Tyrosine KinaseThe 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
2001
Calpain Cleavage Promotes Talin Binding to the β3Integrin Cytoplasmic Domain*
Yan B, Calderwood D, Yaspan B, Ginsberg M. Calpain Cleavage Promotes Talin Binding to the β3Integrin Cytoplasmic Domain*. Journal Of Biological Chemistry 2001, 276: 28164-28170. PMID: 11382782, DOI: 10.1074/jbc.m104161200.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAntigens, CDBiotinBlood PlateletsCalpainCytoplasmCytoskeletonDNA, ComplementaryDose-Response Relationship, DrugGas Chromatography-Mass SpectrometryHumansIntegrin beta3IntegrinsKineticsMolecular Sequence DataPlatelet Membrane GlycoproteinsProtein BindingProtein Structure, TertiaryRatsRecombinant ProteinsSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSurface Plasmon ResonanceTalinTime Factors
1997
The Integrin α1 A-domain Is a Ligand Binding Site for Collagens and Laminin*
Calderwood D, Tuckwell D, Eble J, Kühn K, Humphries M. The Integrin α1 A-domain Is a Ligand Binding Site for Collagens and Laminin*. Journal Of Biological Chemistry 1997, 272: 12311-12317. PMID: 9139675, DOI: 10.1074/jbc.272.19.12311.Peer-Reviewed Original Research
1995
Integrin α2 I-domain is a binding site for collagens
Tuckwell D, Calderwood D, Green L, Humphries M. Integrin α2 I-domain is a binding site for collagens. Journal Of Cell Science 1995, 108: 1629-1638. PMID: 7615681, DOI: 10.1242/jcs.108.4.1629.Peer-Reviewed Original ResearchConceptsAlpha 2 beta 1Alpha 1 beta 1I-domainIntegrin alpha 2 beta 1Beta 1N-terminal regionMajor cellular receptorAlpha 2 subunitIntegrins alpha 1 beta 1Complete receptorBacterial expressionAnti-functional antibodiesCollagen-binding domainA-domainInhibits cellAmino acidsCollagen specificityCellular receptorsXI collagenConcentration-dependent mannerVon Willebrand factorAlpha 1BindingWillebrand factorHomology