2018
Activity of the SPCA1 Calcium Pump Couples Sphingomyelin Synthesis to Sorting of Secretory Proteins in the Trans-Golgi Network
Deng Y, Pakdel M, Blank B, Sundberg EL, Burd CG, von Blume J. Activity of the SPCA1 Calcium Pump Couples Sphingomyelin Synthesis to Sorting of Secretory Proteins in the Trans-Golgi Network. Developmental Cell 2018, 47: 464-478.e8. PMID: 30393074, PMCID: PMC6261503, DOI: 10.1016/j.devcel.2018.10.012.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkTGN membranesCell surface transportProtein sortingTrafficking pathwaysSecretion pathwaySecretory proteinsSphingomyelin synthesisSorting mechanismLipid synthesisProteinVesicular carriersCab45Sphingomyelin contentNew lipidSortingPrincipal functionMembranePathwayCore componentLipidsGolgiSurface transportExportActivityCell-Penetrating Peptide Mediates Intracellular Membrane Passage of Human Papillomavirus L2 Protein to Trigger Retrograde Trafficking
Zhang P, da Silva G, Deatherage C, Burd C, DiMaio D. Cell-Penetrating Peptide Mediates Intracellular Membrane Passage of Human Papillomavirus L2 Protein to Trigger Retrograde Trafficking. Cell 2018, 174: 1465-1476.e13. PMID: 30122350, PMCID: PMC6128760, DOI: 10.1016/j.cell.2018.07.031.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCapsid ProteinsCell-Penetrating PeptidesEndosomesGolgi ApparatusGreen Fluorescent ProteinsHEK293 CellsHeLa CellsHuman papillomavirus 16HumansMutagenesisOncogene Proteins, ViralProtein TransportRecombinant Fusion ProteinsSequence AlignmentVirus AttachmentVirus InternalizationConceptsCell-penetrating peptidesTrans-Golgi networkNormal cell physiologyL2 proteinRetrograde transport pathwayShort protein segmentsHPV L2 proteinTrafficking factorsRetrograde traffickingCationic cell-penetrating peptidesCell physiologyEndosomal membranesProtein segmentsC-terminusBiological roleNon-enveloped virusesRetrograde pathwayL2 capsid proteinsMembrane passageCell penetrating peptideCapsid proteinViral proteinsProteinRetromerTransport pathways
2016
Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle
Deng Y, Rivera-Molina FE, Toomre DK, Burd CG. Sphingomyelin is sorted at the trans Golgi network into a distinct class of secretory vesicle. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: 6677-6682. PMID: 27247384, PMCID: PMC4914164, DOI: 10.1073/pnas.1602875113.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkSynthesis of sphingomyelinGolgi networkSecretory vesiclesPlasma membraneQuantitative live-cell imagingVesicular transport carriersSorting of proteinsGlycophosphatidylinositol-anchored proteinsPore-forming toxinsLive-cell imagingInterorganelle traffickingAbundant sphingolipidIntracellular traffickingSecretory proteinsSM transportTransport carriersProteinCell imagingTraffickingDistinct classesSpecific carrierVesiclesPrincipal functionSorting
2004
Functions of Rab GTPases in organelle biogenesis
Burd C, Collins R. Functions of Rab GTPases in organelle biogenesis. Topics In Current Genetics 2004, 10: 65-88. DOI: 10.1007/b97781.Peer-Reviewed Original ResearchRab GTPasesSpecific effector proteinsVesicle tetheringOrganelle biogenesisMembrane traffickingCargo sortingEffector proteinsEndocytic organellesGTP bindingOrganelle transportGTPasesConformational changesBiogenesisDiverse aspectsRabRecent progressOrganellesTraffickingProteinTetheringBindingSortingFusion
2001
FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*
Shin M, Ogburn K, Varban O, Gilbert P, Burd C. FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*. Journal Of Biological Chemistry 2001, 276: 41388-41393. PMID: 11526110, DOI: 10.1074/jbc.m105665200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceEndosomesGreen Fluorescent ProteinsIntracellular MembranesLigasesLuminescent ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVacuolesConceptsPI3K productsVacuolar membraneFYVE domainUbiquitin ligaseK productRING-type ubiquitin ligaseUbiquitin ligase activityFYVE fingerFinger motifEukaryotic cellsYeast SaccharomycesCellular proteinsRING domainLigase activityDeletional analysisFusion proteinStructural domainsHistidine residuesPrimary structurePI3KFluorescence microscopyProteinLigaseBindsMembrane
2000
Visualizing protein dynamics in yeast with green fluorescent protein
Burd C. Visualizing protein dynamics in yeast with green fluorescent protein. Methods In Enzymology 2000, 327: 61-69. PMID: 11044974, DOI: 10.1016/s0076-6879(00)27267-4.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein dynamicsUse of GFPFluorescent proteinYeast cell biologyProtein sortingRNA localizationIndividual cellular componentsChromosomal dynamicsProtein localizationKinase signalingCell biologyMutant strainMolecular tagsCellular componentsYeastProteinNucleocytoplasmicBroad arrayLocalizationSignalingBiologySortingMajor impactTags
1999
Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain
Kutateladze T, Ogburn K, Watson W, de Beer T, Emr S, Burd C, Overduin M. Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain. Molecular Cell 1999, 3: 805-811. PMID: 10394369, DOI: 10.1016/s1097-2765(01)80013-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesConserved SequenceDimerizationHumansLiposomesMembrane ProteinsMolecular Sequence DataMolecular WeightMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphatidylinositolsProtein BindingProtein FoldingProtein Structure, SecondarySolubilitySubstrate SpecificityVesicular Transport ProteinsZincZinc FingersConceptsFYVE domainEndosome autoantigen 1Membrane trafficking eventsHeteronuclear magnetic resonance spectroscopyZinc-binding motifSpecific amino acidsTrafficking eventsEndosome fusionCellular signalingAlpha-helixBeta hairpinAmino acidsPhosphoinositidePhosphatidylinositolMotifStructural featuresRing fingerDomainPtdlnsSignalingProteinHairpinHelixBroad rangeLipidsMolecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*
Luan P, Balch W, Emr S, Burd C. Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*. Journal Of Biological Chemistry 1999, 274: 14806-14817. PMID: 10329679, DOI: 10.1074/jbc.274.21.14806.Peer-Reviewed Original ResearchConceptsRecycling factorNucleotide Dissociation InhibitorFusion of vesiclesSite-directed mutagenesisAmino acid residuesRab deliveryDistinct RabsRab GTPasesRab proteinsRab-GDPDissociation inhibitorMembrane associationEssential proteinsMolecular dissectionEndocytic pathwayGDI functionAcid residuesRabCellular membranesDominant inhibitionMultiple effectorsRate of recyclingInhibitor functionProteinEndogenous pool
1995
Structure and function of hnRNP proteins
Kiledjian M, Burd C, Gorlach M, Portman D, Dreyfuss G. Structure and function of hnRNP proteins. 1995, 127-149. DOI: 10.1093/oso/9780199635054.003.0006.Peer-Reviewed Original ResearchHnRNP proteinsEukaryotic RNA polymerase IIRNA-processing reactionsRNA polymerase IIRNA-binding proteinNascent transcriptsPolymerase IIHnRNP complexesTranscription complexPrimary transcriptCytoplasmic mRNAPre-mRNAMRNA moleculesGene expressionProteinMRNATranscriptsSeries of eventsNuclear structureComplexesIntransHnRNAsStable componentCytoplasmPathway
1994
The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins.
Görlach M, Burd C, Dreyfuss G. The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins. Journal Of Biological Chemistry 1994, 269: 23074-23078. PMID: 8083209, DOI: 10.1016/s0021-9258(17)31621-6.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesElectrophoresis, Polyacrylamide GelGene AmplificationHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataRibonucleoproteinsRNA, Heterogeneous NuclearRNA-Binding ProteinsSequence Homology, Amino AcidConceptsRNA-binding domainRNA-binding specificityHnRNP C1Selection/amplificationC proteinMinimal RNA-binding domainHeterogeneous nuclear ribonucleoprotein C proteinsHnRNP C proteinsRandom sequence RNARNA-binding propertiesDeterminant of RNAFilter binding assaysRNP motifGeneral RNASpecificity residesC1-binding siteSequence RNAMotif familyRNA ligandsU residuesContiguous stretchesRNAAmino acidsProteinVariable regionsConserved Structures and Diversity of Functions of RNA-Binding Proteins
Burd C, Dreyfuss G. Conserved Structures and Diversity of Functions of RNA-Binding Proteins. Science 1994, 265: 615-621. PMID: 8036511, DOI: 10.1126/science.8036511.Peer-Reviewed Original ResearchThe mRNA Poly(A)-Binding Protein: Localization, Abundance, and RNA-Binding Specificity
Görlach M, Burd C, Dreyfuss G. The mRNA Poly(A)-Binding Protein: Localization, Abundance, and RNA-Binding Specificity. Experimental Cell Research 1994, 211: 400-407. PMID: 7908267, DOI: 10.1006/excr.1994.1104.Peer-Reviewed Original ResearchConceptsHuman PABPRNA binding specificityQuantitative immunoblotting experimentsMost eukaryotic mRNAsRNA-binding propertiesTranslation of mRNAsConfocal immunofluorescence microscopySelection/amplificationEukaryotic mRNAsOligonucleotide poolRNA sequencesRich sequencesCellular localizationBinding proteinHeLa cellsImmunofluorescence microscopyImmunoblotting experimentsLow turnover rateLow affinityPABPProteinAbundanceMRNAIntracellular concentrationTurnover rate
1993
The hnRNP proteins
Görlach M, Burd C, Portman D, Dreyfuss G. The hnRNP proteins. Molecular Biology Reports 1993, 18: 73-78. PMID: 8232298, DOI: 10.1007/bf00986759.Peer-Reviewed Original Research
1992
RNA binding characteristics of a 16 kDa glycine‐rich protein from maize
Ludevid M, Freire M, Gómez J, Burd C, Albericio F, Giralt E, Dreyfuss G, Pagès M. RNA binding characteristics of a 16 kDa glycine‐rich protein from maize. The Plant Journal 1992, 2: 999-1003. PMID: 1302645, DOI: 10.1046/j.1365-313x.1992.t01-10-00999.x.Peer-Reviewed Original ResearchConceptsConsensus sequence-type RNA-binding domainStress responseGlycine-rich proteinRNA-binding domainGuanosine-rich RNAsRNA-binding proteinRNA metabolismProtein bindsLate embryogenesisMature embryosProteinLikely roleRNAMaizeEmbryogenesisEmbryosPlantsBindsMA16MRNASequenceMetabolismAssaysUridineResponse
1989
Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts.
Burd C, Swanson M, Görlach M, Dreyfuss G. Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 9788-9792. PMID: 2557628, PMCID: PMC298587, DOI: 10.1073/pnas.86.24.9788.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA Transposable ElementsDNA, NeoplasmElectrophoresis, Gel, Two-DimensionalHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular Sequence DataProtein BiosynthesisRestriction MappingRibonucleoproteinsRNA, Heterogeneous NuclearSequence Homology, Nucleic AcidSoftwareTransfectionConceptsAmino acid sequenceCS-RBDsHeterogeneous nuclear ribonucleoprotein A2C2 proteinAmino acidsAcid sequenceDiversity of RNAHnRNP protein A1Amino acid identityAuxiliary domainHnRNP proteinsMRNA splicingProtein cDNAAcid identityCarboxyl terminusAmino terminusPrimary structureProtein A1Frame insertsB1 proteinCDNALarge familyProteinRNATerminus