1999
The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*
Rosenthal J, Chen H, Slepnev V, Pellegrini L, Salcini A, Di Fiore P, De Camilli P. The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*. Journal Of Biological Chemistry 1999, 274: 33959-33965. PMID: 10567358, DOI: 10.1074/jbc.274.48.33959.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCoated VesiclesCricetinaeDNA, ComplementaryFluorescent Antibody TechniqueGene ExpressionHumansIntracellular Signaling Peptides and ProteinsLuciferasesMaleMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsPhylogenyProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue DistributionVesicular Transport ProteinsConceptsEpsin 1Clathrin coatClathrin adaptor AP-2New protein modulesNew protein familyTerminal regionAdaptor AP-2Family of proteinsRat brain libraryNPF motifsProtein modulesProtein familyCell peripheryAP-2Membrane dynamicsSimilar proteinsBrain libraryClathrinEps15Vesicle fractionEpsinGreen fluorescentGolgi regionCell surfaceProteinTNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1.
Jones S, Ledgerwood E, Prins J, Galbraith J, Johnson D, Pober J, Bradley J. TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1. The Journal Of Immunology 1999, 162: 1042-8. PMID: 9916731, DOI: 10.4049/jimmunol.162.2.1042.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDAortaBrefeldin ACattleCell CompartmentationCell Line, TransformedCell MembraneEndothelium, VascularGolgi ApparatusHumansMicroscopy, ConfocalProteinsReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISubcellular FractionsTNF Receptor-Associated Factor 1TransfectionTumor Necrosis Factor-alphaU937 CellsConceptsTrans-Golgi networkPlasma membraneTNF-R1Golgi regionConfocal immunofluorescence microscopyHuman endothelial cell line ECV304Endothelial cell line ECV304Receptor-mediated endocytosisAdaptor proteinSubcellular localizationSubcellular locationCell fractionationBovine aortic endothelial cellsCoimmunoprecipitation studiesEndothelial cellsTRADDCell line U937Golgi apparatusSubcellular interactionsWestern blot analysisCell extractsMonocyte cell line U937Expression plasmidGolgiImmunofluorescence microscopy
1997
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *
Garcı́a-Cardeña G, Martasek P, Masters B, Skidd P, Couet J, Li S, Lisanti M, Sessa W. Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *. Journal Of Biological Chemistry 1997, 272: 25437-25440. PMID: 9325253, DOI: 10.1074/jbc.272.41.25437.Peer-Reviewed Original ResearchConceptsCaveolin-1Peripheral membrane proteinsInteraction of eNOSC-terminal tailAmino acids 310Direct interactionCo-transfection experimentsSite-directed mutagenesisNovel functional roleEndothelial nitric oxide synthaseMolecular chaperonesCytoplasmic domainCaveolin isoformsDeletion mutantsMammalian cellsEndothelial cell lysatesGlutathione S-transferaseMembrane proteinsCaveolin-2Coat proteinNegative regulationCaveolin-3Endothelial cellsDirect bindingGolgi regionThe First 35 Amino Acids and Fatty Acylation Sites Determine the Molecular Targeting of Endothelial Nitric Oxide Synthase into the Golgi Region of Cells: A Green Fluorescent Protein Study
Liu J, Hughes T, Sessa W. The First 35 Amino Acids and Fatty Acylation Sites Determine the Molecular Targeting of Endothelial Nitric Oxide Synthase into the Golgi Region of Cells: A Green Fluorescent Protein Study. Journal Of Cell Biology 1997, 137: 1525-1535. PMID: 9199168, PMCID: PMC2137822, DOI: 10.1083/jcb.137.7.1525.Peer-Reviewed Original ResearchConceptsPalmitoylation-deficient mutantN-myristoylationNIH 3T3 cellsMembrane associationGolgi regionPalmitoylation sitesAmino acidsGreen fluorescent protein studiesGolgi complexFatty acylation sitesGFP fusion proteinBiochemical studiesFluorescent protein chimerasDiffuse fluorescence patternEndothelial cellsEndothelial nitric oxide synthaseCytosolic natureGFP tagFatty acylationAcylated proteinsGolgi markersProtein chimerasIntracellular membranesAcylation siteIntracellular targeting
1990
A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV
Yannariello-Brown J, Madri J. A 48 kDa collagen-binding phosphoprotein isolated from bovine aortic endothelial cells interacts with the collagenous domain, but not the globular domain, of collagen type IV. Biochemical Journal 1990, 265: 383-392. PMID: 2154186, PMCID: PMC1136898, DOI: 10.1042/bj2650383.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAortaCattleCell MembraneCells, CulturedChromatography, AffinityChymotrypsinCollagenElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEndothelium, VascularFluorescent Antibody TechniqueImmune SeraMolecular WeightPeptide MappingPhosphoproteinsReceptors, Cell SurfaceReceptors, CollagenConceptsBovine aortic endothelial cellsSDS/PAGENon-equilibrium pH gel electrophoresisCollagen type IVCollagenous domainTwo-dimensional gel systemAortic endothelial cellsAdhesion assaysCell surface populationIndirect immunofluorescence experimentsGlobular NC1 domainCell surface labelingCollagen-binding proteinsChymotryptic peptide mapsEndothelial cellsGlobular domainIntracellular transportMinor isoformIndividual isoformsImmunofluorescence experimentsMolecular massGolgi regionCollagenous regionCell surfacePeptide maps
1985
Incorporation of a Charged Amino Acid into the Membrane-Spanning Domain Blocks Cell Surface Transport But Not Membrane Anchoring of a Viral Glycoprotein
Adams G, Rose J. Incorporation of a Charged Amino Acid into the Membrane-Spanning Domain Blocks Cell Surface Transport But Not Membrane Anchoring of a Viral Glycoprotein. Molecular And Cellular Biology 1985, 5: 1442-1448. DOI: 10.1128/mcb.5.6.1442-1448.1985.Peer-Reviewed Original ResearchMembrane anchoringG proteinsAmino acidsCell surfaceIsoleucine residueMembrane-spanning domainsCell surface transportVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisAmino acid sequenceUncharged amino acidsDetectable protein levelsHydrophobic amino acidsAnimal cellsCDNA clonesIntracellular membranesAcid sequencePunctate patternGolgi regionProteinContinuous stretchVesicular patternProtein levelsViral glycoproteinsVirus glycoproteinIncorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein.
Adams G, Rose J. Incorporation of a charged amino acid into the membrane-spanning domain blocks cell surface transport but not membrane anchoring of a viral glycoprotein. Molecular And Cellular Biology 1985, 5: 1442-1448. PMID: 2993864, PMCID: PMC366875, DOI: 10.1128/mcb.5.6.1442.Peer-Reviewed Original ResearchConceptsMembrane anchoringG proteinsAmino acidsCell surfaceIsoleucine residueMembrane-spanning domainsCell surface transportVesicular stomatitis virus glycoproteinOligonucleotide-directed mutagenesisAmino acid sequenceUncharged amino acidsDetectable protein levelsHydrophobic amino acidsAnimal cellsCDNA clonesIntracellular membranesAcid sequencePunctate patternGolgi regionProteinContinuous stretchVesicular patternProtein levelsViral glycoproteinsVirus glycoprotein
1965
The fine structure of differentiating interstitial cells in Hydra
Lentz T. The fine structure of differentiating interstitial cells in Hydra. Cell And Tissue Research 1965, 67: 547-560. PMID: 4380169, DOI: 10.1007/bf00342586.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumGolgi apparatusGolgi regionRough-surfaced endoplasmic reticulumNematocyst formationDigestive cellsGolgi vesiclesBundles of filamentsCell differentiationUndifferentiated cellsGland cellsCytoplasmic organellesInterstitial cellsReticulumFree ribosomesSecretory granulesHydraMinute tubulesModel systemNematocystsCnidoblastsCellsCytoplasmic processesSmall undifferentiated cellsRibosomes
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