2023
Three-dimensional structured illumination microscopy with enhanced axial resolution
Li X, Wu Y, Su Y, Rey-Suarez I, Matthaeus C, Updegrove T, Wei Z, Zhang L, Sasaki H, Li Y, Guo M, Giannini J, Vishwasrao H, Chen J, Lee S, Shao L, Liu H, Ramamurthi K, Taraska J, Upadhyaya A, La Riviere P, Shroff H. Three-dimensional structured illumination microscopy with enhanced axial resolution. Nature Biotechnology 2023, 41: 1307-1319. PMID: 36702897, PMCID: PMC10497409, DOI: 10.1038/s41587-022-01651-1.Peer-Reviewed Original Research
2021
Live imaging and quantitation of nascent transcription using the MS2/MCP system in the Drosophila embryo
Hoppe C, Ashe HL. Live imaging and quantitation of nascent transcription using the MS2/MCP system in the Drosophila embryo. STAR Protocols 2021, 2: 100379. PMID: 33778778, PMCID: PMC7982776, DOI: 10.1016/j.xpro.2021.100379.Peer-Reviewed Original Research
2018
Lipid trafficking by yeast Snx4 family SNX-BAR proteins promotes autophagy and vacuole membrane fusion
Ma M, Kumar S, Purushothaman L, Babst M, Ungermann C, Chi RJ, Burd CG. Lipid trafficking by yeast Snx4 family SNX-BAR proteins promotes autophagy and vacuole membrane fusion. Molecular Biology Of The Cell 2018, 29: 2190-2200. PMID: 29949447, PMCID: PMC6249802, DOI: 10.1091/mbc.e17-12-0743.Peer-Reviewed Original ResearchConceptsVacuole fusionAutophagy pathwaySNX-BAR proteinsCore autophagy machinerySelective autophagy pathwaysHomotypic vacuole fusionVacuole membrane fusionPhosphatidylserine-containing membranesRetrograde transport carriersTurnover of macromoleculesAutophagy intermediatesGlycerophospholipid homeostasisNonselective autophagyBAR domainEndosomal sortingAutophagy machineryFusion competenceLipid traffickingPhosphatidylserine-rich membranesCoat proteinMembrane fusionVacuole membranePhosphatidylethanolamine biosynthesisYeast cellsPhosphatidylethanolamine synthesis
2016
An RNA-aptamer-based two-color CRISPR labeling system
Wang S, Su JH, Zhang F, Zhuang X. An RNA-aptamer-based two-color CRISPR labeling system. Scientific Reports 2016, 6: 26857. PMID: 27229896, PMCID: PMC4882555, DOI: 10.1038/srep26857.Peer-Reviewed Original ResearchConceptsSingle guide RNAsDifferent fluorescent proteinsGenomic lociFluorescent proteinSpecific chromatin lociEndogenous genomic lociDynamics of chromatinPP7 coat proteinTarget genomic lociStem loop 2Essential biological functionsSpecific DNA sequencesDifferent bacterial speciesChromatin imagingCRISPR single guide RNAsChromatin lociRepetitive sequencesDNA sequencesChromatin labelingCoat proteinBiological functionsHuman cellsLoop 2RNA aptamersBacterial speciesMammalian African trypanosome VSG coat enhances tsetse’s vector competence
Aksoy E, Vigneron A, Bing X, Zhao X, O'Neill M, Wu YN, Bangs JD, Weiss BL, Aksoy S. Mammalian African trypanosome VSG coat enhances tsetse’s vector competence. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 6961-6966. PMID: 27185908, PMCID: PMC4922192, DOI: 10.1073/pnas.1600304113.Peer-Reviewed Original ResearchConceptsVariant surface glycoproteinPeritrophic matrixMammalian hostsVector competenceTranscription factor familyMidgut homeostasisTsetse midgutTrypanosome biologyFactor familyPM barrierCoat proteinNovel functionAfrican trypanosomesTsetse vectorInfection processParasite developmentAnimal trypanosomiasesAntigenic variationVSG moleculesVSG coatBiological vectorsMidgutProtozoan parasiteDisease transmissionTsetse flies
2012
AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus
Lee N, Pimienta G, Steitz JA. AUF1/hnRNP D is a novel protein partner of the EBER1 noncoding RNA of Epstein-Barr virus. RNA 2012, 18: 2073-2082. PMID: 23012480, PMCID: PMC3479396, DOI: 10.1261/rna.034900.112.Peer-Reviewed Original ResearchMeSH Keywords3' Untranslated RegionsAptamers, NucleotideAU Rich ElementsBinding, CompetitiveCell Line, TumorHerpesvirus 4, HumanHeterogeneous Nuclear Ribonucleoprotein D0Heterogeneous-Nuclear Ribonucleoprotein DHost-Pathogen InteractionsHumansImmunoprecipitationMutagenesis, InsertionalProtein BindingProtein IsoformsRNA StabilityRNA, ViralConceptsAU-rich elementsProtein partnersAUF1/hnRNP DUntranslated regionBacteriophage MS2 coat proteinNovel protein partnersHigh abundanceElectrophoretic mobility shift assaysEpstein-Barr virusMS2 coat proteinStable isotope labelingMobility shift assaysInteracting proteinMolecular functionsHnRNP DAlternative splicingNoncoding RNAsShift assaysCoat proteinIsotope labelingP40 isoformRNA aptamersRNA 1AUF1UV crosslinking
2010
Association with β-COP Regulates the Trafficking of the Newly Synthesized Na,K-ATPase*
Morton MJ, Farr GA, Hull M, Capendeguy O, Horisberger JD, Caplan MJ. Association with β-COP Regulates the Trafficking of the Newly Synthesized Na,K-ATPase*. Journal Of Biological Chemistry 2010, 285: 33737-33746. PMID: 20801885, PMCID: PMC2962472, DOI: 10.1074/jbc.m110.141119.Peer-Reviewed Original ResearchConceptsK-ATPase αK-ATPase β-subunitΒ-COPΒ-subunitΑ-subunitPlasma membraneEndoplasmic reticulumK-ATPase α-subunitMutant α-subunitsIon-transporting ATPasePlasma membrane expressionK-ATPasePulse-chase experimentsPartner proteinsNovel labeling techniqueCoat proteinDibasic motifCell surfaceMembrane expressionObligate intermediateΒ subunit expressionProteinReticulumP22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical Crosslinks
Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS. P22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical Crosslinks. Structure 2010, 18: 390-401. PMID: 20223221, PMCID: PMC2951021, DOI: 10.1016/j.str.2009.12.014.Peer-Reviewed Original ResearchConceptsP22 coat proteinCoat proteinAuxiliary proteinsCoat protein structureCryo-electron microscopyN-terminal helixBacteriophage P22 coat proteinViral capsid assemblyDsDNA phagesPseudoatomic modelCapsid maturationP-loopProtein structureCapsid stabilizationIntersubunit interactionsCapsid assemblyComparative modelingNovel mechanismProteinTrypsin digestionSubunit additionGold labelingChemical crosslinksMaturationAssembly
2003
Structure and dynamics of a membrane protein in micelles from three solution NMR experiments
Lee S, Mesleh MF, Opella SJ. Structure and dynamics of a membrane protein in micelles from three solution NMR experiments. Journal Of Biomolecular NMR 2003, 26: 327-334. PMID: 12815259, DOI: 10.1023/a:1024047805043.Peer-Reviewed Original ResearchConceptsMembrane proteinsSolution NMR experimentsPISA wheelsLoop regionDipolar wavesResidual dipolar couplingsBackbone amide resonancesPf1 coat proteinHigh-throughput structural characterizationHeteronuclear NOE experimentsMembrane-bound formHydrophobic helicesHMQC-NOESY experimentsAmphipathic helixCoat proteinNMR experimentsMobile residuesHelical residuesBackbone dynamicsChemical shift anisotropyProteinAmide resonancesHelixResidual chemical shift anisotropyDipolar couplings
2000
In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation
Bucci M, Gratton J, Rudic R, Acevedo L, Roviezzo F, Cirino G, Sessa W. In vivo delivery of the caveolin-1 scaffolding domain inhibits nitric oxide synthesis and reduces inflammation. Nature Medicine 2000, 6: 1362-1367. PMID: 11100121, DOI: 10.1038/82176.Peer-Reviewed Original ResearchConceptsCaveolin-1Signal transductionSmall-molecule mimicryCaveolae assemblyInternalization sequenceCoat proteinEndothelial cellsPhysiological importanceEndothelial nitric oxide synthase (eNOS) inhibitorTransductionCholesterol transportNitric oxide synthase inhibitorChimeric peptideInhibits nitric oxide synthesisOxide synthase inhibitorNitric oxide synthesisNew therapeutic approachesNitric oxide productionSelective inhibitionDomainPeptidesCaveolinAcute inflammationCellsSystemic administrationTandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*
Slepnev V, Ochoa G, Butler M, De Camilli P. Tandem Arrangement of the Clathrin and AP-2 Binding Domains in Amphiphysin 1 and Disruption of Clathrin Coat Function by Amphiphysin Fragments Comprising These Sites*. Journal Of Biological Chemistry 2000, 275: 17583-17589. PMID: 10748223, DOI: 10.1074/jbc.m910430199.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsBinding SitesBinding, CompetitiveCHO CellsClathrinCricetinaeGlutathione TransferaseHumansMembrane ProteinsMolecular Sequence DataMonomeric Clathrin Assembly ProteinsMutagenesis, Site-DirectedNerve Tissue ProteinsPeptide FragmentsRecombinant Fusion ProteinsTransfectionConceptsAP-2Amphiphysin 1Coat proteinClathrin adaptor AP-2COOH-terminal SH3 domainAdaptor AP-2Chinese hamster ovary cellsCoat functionMultifunctional adaptorSH3 domainHamster ovary cellsTerminal domainBinding domainsClathrinDynaminMembrane lipidsAmphiphysinSynaptic vesiclesAmino acidsSynaptojaninOvary cellsDirect interactionProteinTertiary complexTandem arrangement
1999
The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*
Lai M, Hong J, Ruggiero A, Burnett P, Slepnev V, De Camilli P, Snyder S. The Calcineurin-Dynamin 1 Complex as a Calcium Sensor for Synaptic Vesicle Endocytosis*. Journal Of Biological Chemistry 1999, 274: 25963-25966. PMID: 10473536, DOI: 10.1074/jbc.274.37.25963.Peer-Reviewed Original ResearchConceptsCalcium sensorEndocytic coat proteinsSynaptic endocytic machinerySynaptic vesicle endocytosisSynaptic vesiclesCalcium-dependent phosphatase calcineurinEndocytic machineryVesicle endocytosisDynamin 1Phosphatase calcineurinCoat proteinCalcium-dependent formationCalcium-sensing mechanismPhysical associationEndocytosisVesiclesCalcium-dependent processesClathrinSynaptotagminComplexesExocytosisCalcineurinMachineryProteinCodistribution of NOS and caveolin throughout peripheral vasculature and skeletal muscle of hamsters
Segal S, Brett S, Sessa W. Codistribution of NOS and caveolin throughout peripheral vasculature and skeletal muscle of hamsters. American Journal Of Physiology 1999, 277: h1167-h1177. PMID: 10484439, DOI: 10.1152/ajpheart.1999.277.3.h1167.Peer-Reviewed Original ResearchConceptsCaveolin-3Caveolin-1Skeletal muscleCaveolin isoformsCoat proteinCaveolinFunctional interactionIntact organismEnzyme isoformsNitric oxide synthase activitySmooth muscle cellsMuscle fibersOxide synthase activityVascular smooth muscleSynthase activitySkeletal muscle fibersMuscle cellsIsoformsCell systemSystemic vasculatureVena cavaFemoral arteryAbdominal aortaPeripheral vasculatureEndothelial cells
1998
Novel pathways, membrane coats and PI kinase regulation in yeast lysosomal trafficking
Burd C, Babst M, Emr S. Novel pathways, membrane coats and PI kinase regulation in yeast lysosomal trafficking. Seminars In Cell And Developmental Biology 1998, 9: 527-533. PMID: 9835640, DOI: 10.1006/scdb.1998.0255.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAlkaline PhosphataseBiological TransportCarboxypeptidasesCarrier ProteinsCathepsin ACell MembraneCoated Pits, Cell-MembraneFungal ProteinsIntracellular MembranesLysosomesMembrane ProteinsModels, BiologicalMonomeric Clathrin Assembly ProteinsPhosphatidylinositol 3-KinasesSaccharomyces cerevisiaeVacuolesConceptsSorting pathwaysVesicle docking/fusionAdaptor protein-3 complexProtein sorting signalsDocking/fusionPhosphorylation-dependent ubiquitinationVesicle coat proteinsYeast Saccharomyces cerevisiaeMembrane fusion reactionGolgi recyclingEndocytic cargoFYVE domainSorting signalsKinase regulationEukaryotic cellsImportant mechanistic insightsMembrane transport reactionsRecycling pathwaySaccharomyces cerevisiaeBiosynthetic pathwayCoat proteinRecognition motifMembrane coatMolecular mechanismsLysosomal traffickingADP ribosylation factor regulates spectrin binding to the Golgi complex
Godi A, Santone I, Pertile P, Devarajan P, Stabach P, Morrow J, Di Tullio G, Polishchuk R, Petrucci T, Luini A, De Matteis M. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 8607-8612. PMID: 9671725, PMCID: PMC21123, DOI: 10.1073/pnas.95.15.8607.Peer-Reviewed Original ResearchConceptsADP-ribosylation factorGolgi complexRibosylation factorG proteinsVesicular stomatitis virus G proteinPleckstrin homology domainSmall G proteinsPH domain interactionBinding of spectrinVirus G proteinGolgi spectrinHomology domainPH domainCoat proteinDocking siteDomain interactionsGolgiEndoplasmic reticulumPtdInsP2 levelsDomain IPhospholipase DSpectrinGolgi fractionsProteinPtdInsP2Generation of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes
Takei K, Haucke V, Slepnev V, Farsad K, Salazar M, Chen H, De Camilli P. Generation of Coated Intermediates of Clathrin-Mediated Endocytosis on Protein-Free Liposomes. Cell 1998, 94: 131-141. PMID: 9674434, DOI: 10.1016/s0092-8674(00)81228-3.Peer-Reviewed Original Research
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 region
1996
Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*
García-Cardeña G, Fan R, Stern D, Liu J, Sessa W. Endothelial Nitric Oxide Synthase Is Regulated by Tyrosine Phosphorylation and Interacts with Caveolin-1*. Journal Of Biological Chemistry 1996, 271: 27237-27240. PMID: 8910295, DOI: 10.1074/jbc.271.44.27237.Peer-Reviewed Original ResearchConceptsNovel regulatory mechanismTyrosine phosphorylationCaveolin-1Bovine aortic endothelial cellsRegulatory mechanismsProtein tyrosine phosphatase inhibitorCaveolin-interacting proteinsPhosphoamino acid analysisTyrosine phosphatase inhibitorTreatment of BAECBovine lung microvascular endothelial cellsEndothelial nitric oxide synthaseSubcellular traffickingPhosphatase inhibitorCoat proteinEndothelial cellsMetabolic labelingSodium orthovanadatePhosphorylationCaveolaeAortic endothelial cellsLung microvascular endothelial cellsProteinAcid analysisImmunoprecipitationReceptor signalling and the regulation of endocytic membrane transport
Seaman M, Burd C, Emr S. Receptor signalling and the regulation of endocytic membrane transport. Current Opinion In Cell Biology 1996, 8: 549-556. PMID: 8791448, DOI: 10.1016/s0955-0674(96)80034-2.Peer-Reviewed Original ResearchConceptsPlasma membraneDifferent protein-protein interactionsEndocytic membrane transportReceptor signalingCell surface receptor signalingVesicle coat proteinsProtein-protein interactionsLayer of regulationRegulation of proteinsSignal transduction pathwaysSurface receptor signalingReceptor tyrosine kinasesMembrane trafficMembrane traffickingSecond messenger cascadesCoat proteinPotential new roleMolecular mechanismsTyrosine kinaseMembrane transportCell surfaceRecent evidenceMessenger cascadesCritical roleRegulation
1974
Specific recognition of the isolated R17 replicase initiator region by R17 coat protein
STEITZ J. Specific recognition of the isolated R17 replicase initiator region by R17 coat protein. Nature 1974, 248: 223-225. PMID: 4819415, DOI: 10.1038/248223a0.Peer-Reviewed Original Research
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