2024
Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis
Parolek J, Burd C. Bridge-like lipid transfer protein family member 2 suppresses ciliogenesis. Molecular Biology Of The Cell 2024, 35: br11. PMID: 38536441, PMCID: PMC11151097, DOI: 10.1091/mbc.e24-02-0065.Peer-Reviewed Original ResearchConceptsLipid transfer proteinsFamily member 2RPE-1 cellsSuppressed ciliogenesisTubular endosomal networkMembrane contact sitesNegative regulator of ciliogenesisRegulator of ciliogenesisDrosophila melanogaster</i>Evolutionary conserved proteinMember 2Primary cilium biogenesisRPE-1Endosomal networkGenetic interactionsTubular endosomesCilium biogenesisProtein familyStructure predictionContact sitesEndoplasmic reticulumDomain-containingPreweaning lethalityNegative regulatorCiliogenesis
2019
Syndecan-1 Mediates Sorting of Soluble Lipoprotein Lipase with Sphingomyelin-Rich Membrane in the Golgi Apparatus
Sundberg EL, Deng Y, Burd CG. Syndecan-1 Mediates Sorting of Soluble Lipoprotein Lipase with Sphingomyelin-Rich Membrane in the Golgi Apparatus. Developmental Cell 2019, 51: 387-398.e4. PMID: 31543446, PMCID: PMC6832887, DOI: 10.1016/j.devcel.2019.08.014.Peer-Reviewed Original ResearchConceptsTrans-Golgi networkSphingomyelin-rich membranesTransmembrane domainSecretory pathwayVesicular transport carriersIntegral membrane proteinsProtein transmembrane domainBiosynthetic secretory pathwaySyndecan-1Heparan sulfate chainsLipoprotein lipaseSorting receptorSecretion pathwayMembrane proteinsGolgi membranesProteoglycan syndecan-1Protein cargoSecretory vesiclesPlasma membraneGolgi apparatusSpecific sequencesTransport carriersSulfate chainsLipid compositionEnzyme lipoprotein lipase
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
2000
Determinants of NPC1 Expression and Action: Key Promoter Regions, Posttranscriptional Control, and the Importance of a “Cysteine-Rich” Loop
Watari H, Blanchette-Mackie E, Dwyer N, Watari M, Burd C, Patel S, Pentchev P, Strauss J. Determinants of NPC1 Expression and Action: Key Promoter Regions, Posttranscriptional Control, and the Importance of a “Cysteine-Rich” Loop. Experimental Cell Research 2000, 259: 247-256. PMID: 10942596, DOI: 10.1006/excr.2000.4976.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarcinoma, HepatocellularCarrier ProteinsCHO CellsCricetinaeCysteineGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsLysosomesMembrane GlycoproteinsNiemann-Pick C1 ProteinNiemann-Pick DiseasesPlasmidsProgesteronePromoter Regions, GeneticProtein Structure, TertiaryProteinsRNA Processing, Post-TranscriptionalRNA, MessengerTransfectionTumor Cells, CulturedZincConceptsNiemann-Pick type C diseaseCholesterol trafficking defectType C diseaseC diseaseNPC1 expressionTrafficking defectsNPC1 genePromoter activityMajor transcription initiation siteBase pairsLate endosomal compartmentsTranscription initiation siteTranscription start siteI1061T mutationKey promoter regionChinese hamster cell lineProgesterone-treated cellsHamster cell linesNPC1 mRNA levelsProgesterone-induced increaseZinc-binding activityProtein synthesis inhibitorCT60 cellsThreonine residuesPosttranscriptional regulation
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 rangeLipids
1996
A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins
Burd C, Mustol P, Schu P, Emr S. A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins. Molecular And Cellular Biology 1996, 16: 2369-2377. PMID: 8628304, PMCID: PMC231225, DOI: 10.1128/mcb.16.5.2369.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceAnimalsCarrier ProteinsCloning, MolecularFungal ProteinsGenes, FungalGenetic Complementation TestGuanine Nucleotide Exchange FactorsHumansMammalsMolecular Sequence DataMutagenesisPolymerase Chain ReactionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTemperatureVacuolesVesicular Transport ProteinsConceptsVacuolar protein sortingProtein sortingVacuolar proteinVPS pathwayVacuolar protein sorting (VPS) genesTemperature-sensitive growth defectTemperature-conditional alleleVacuolar protein precursorsFamily of proteinsSecretion of proteinsRab GTPaseRA-binding proteinsTransport vesiclesYeast proteinsHomology domainYeast SaccharomycesGrowth defectHuman proteinsVps9pDNA sequencesGene productsCytosolic proteinsNonpermissive temperatureCarboxypeptidase YIntracellular transport
1994
Conserved 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 ResearchhnRNP Proteins and the Biogenesis of mRNA
Dreyfuss G, Matunis M, Piñol-Roma S, Burd C. hnRNP Proteins and the Biogenesis of mRNA. Annual Review Of Biochemistry 1993, 62: 289-321. PMID: 8352591, DOI: 10.1146/annurev.bi.62.070193.001445.Peer-Reviewed Original Research
1991
The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.
Burd C, Matunis E, Dreyfuss G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Molecular And Cellular Biology 1991, 11: 3419-3424. PMID: 1675426, PMCID: PMC361068, DOI: 10.1128/mcb.11.7.3419.Peer-Reviewed Original Research
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