2003
Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling
Calderwood DA, Fujioka Y, de Pereda JM, García-Alvarez B, Nakamoto T, Margolis B, McGlade CJ, Liddington RC, Ginsberg MH. Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 2272-2277. PMID: 12606711, PMCID: PMC151330, DOI: 10.1073/pnas.262791999.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDatabases as TopicDNADose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelGlutathione TransferaseHumansIntegrin beta ChainsIntegrinsMiceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationPhosphorylationPhosphotyrosinePrecipitin TestsProtein BindingProtein ConformationProtein Structure, TertiaryRecombinant Fusion ProteinsRecombinant ProteinsSequence Homology, Amino AcidSignal TransductionTransfectionTyrosineConceptsIntegrin beta tailsBeta tailsPTB domainIntegrin tailsDok-1Heterodimeric integrin adhesion receptorsBiological functionsDomain interactionsPTB domain-containing proteinsDomain-containing proteinsDomain-ligand interactionsPhosphotyrosine-binding (PTB) domainPhosphotyrosine-binding domainCytoplasmic domain interactionsIntegrin-binding proteinsIntegrin adhesion receptorsIntegrin alpha IIbNPXY motifProtein modulesCytoplasmic domainCytoplasmic proteinsAlpha IIbCytoskeletal proteinsCanonical recognition sequenceInteracting residues
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 Kinase
2001
PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase
Formstecher E, Ramos J, Fauquet M, Calderwood D, Hsieh J, Canton B, Nguyen X, Barnier J, Camonis J, Ginsberg M, Chneiweiss H. PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase. Developmental Cell 2001, 1: 239-250. PMID: 11702783, DOI: 10.1016/s1534-5807(01)00035-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActive Transport, Cell NucleusAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsBlotting, NorthernCell DivisionCell NucleusCell SurvivalCHO CellsCricetinaeCytoplasmDNA, ComplementaryDose-Response Relationship, DrugGreen Fluorescent ProteinsImmunohistochemistryLuminescent ProteinsMAP Kinase Signaling SystemMiceMicroscopy, FluorescenceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesModels, BiologicalMolecular Sequence DataMutationPhosphoproteinsPrecipitin TestsProtein BindingSequence Homology, Amino AcidTime FactorsTranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsERK MAP kinasePEA-15MAP kinaseERK nuclear localizationNuclear export sequenceERK-dependent transcriptionMAP kinase pathwayMultiple cell typesERK 1/2 MAP kinase pathwayExport sequenceSubcellular localizationNuclear localizationCytoplasmic sequestrationKinase pathwayIntegrin functionCell typesCell growthKinaseBiological outcomesCell proliferationGenetic deletionTranscriptionERKLocalizationProliferation