1996
Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains.
Rodgers W, Rose J. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. Journal Of Cell Biology 1996, 135: 1515-1523. PMID: 8978819, PMCID: PMC2133949, DOI: 10.1083/jcb.135.6.1515.Peer-Reviewed Original ResearchConceptsExclusion of CD45Low kinase activityGEM fractionMembrane domainsKinase activitySrc family tyrosine kinasesReservoir of enzymesSpecific membrane domainsActivity of p56lckTyrosine phosphatase CD45Family tyrosine kinasesT cell developmentTX-100-soluble fractionGEM domainsPhosphatase CD45Membrane proteinsKinase specific activityLckTyrosine kinaseMembrane fractionJurkat cellsPeptide mappingP56lckPhosphorylationHyperphosphorylation
1994
Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction.
Rodgers W, Crise B, Rose J. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. PMID: 8035816, PMCID: PMC359057, DOI: 10.1128/mcb.14.8.5384.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell CompartmentationDNA PrimersGlycolipidsGlycosylphosphatidylinositolsHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataMutagenesis, Site-DirectedMyristatesPalmitatesProteinsProtein-Tyrosine KinasesStructure-Activity RelationshipConceptsProtein tyrosine kinasesCertain protein tyrosine kinasesTyrosine kinaseMembrane fractionSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorGlycosyl phosphatidylinositolKinaseP56lckCell typesHeLa cellsMDCK cellsGPIProteinGentle disruption
1992
Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.
Crise B, Rose J. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. Journal Of Biological Chemistry 1992, 267: 13593-13597. PMID: 1618861, DOI: 10.1016/s0021-9258(18)42253-3.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomain
1990
Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase.
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. PMID: 2109184, PMCID: PMC360530, DOI: 10.1128/mcb.10.5.1853.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, Differentiation, T-LymphocyteBase SequenceCD4 AntigensCD8 AntigensCysteineCytoplasmDNA Mutational AnalysisHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataProtein BindingProtein-Tyrosine KinasesSignal TransductionStructure-Activity RelationshipConceptsAmino-terminal domainTyrosine protein kinaseCytoplasmic domainProtein kinaseBinding of p56lckCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationCD8 alphaAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsAlpha proteinRelated sequencesAcid residuesCD4 sequencesP56lckGlycoprotein CD4HeLa cellsProteinKinase
1989
The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResidues