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
2022
Pathogenic variants of sphingomyelin synthase SMS2 disrupt lipid landscapes in the secretory pathway
Sokoya T, Parolek J, Foged M, Danylchuk D, Bozan M, Sarkar B, Hilderink A, Philippi M, Botto L, Terhal P, Mäkitie O, Piehler J, Kim Y, Burd C, Klymchenko A, Maeda K, Holthuis J. Pathogenic variants of sphingomyelin synthase SMS2 disrupt lipid landscapes in the secretory pathway. ELife 2022, 11: e79278. PMID: 36102623, PMCID: PMC9531943, DOI: 10.7554/elife.79278.Peer-Reviewed Original ResearchConceptsSecretory pathwayER export signalPatient-derived fibroblastsFull enzymatic activityPhysical membrane propertiesExport signalSterol gradientLipid landscapeMammalian cellsCholesterol organizationLipid orderEnzymatic activityLipid distributionOsteogenic cellsPathwayBone phenotypeSMS2Glycerophospholipid profilePathogenic variantsCellsVariantsSphingomyelinSkeletal dysplasiaERSphingolipids
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 regulationVisualizing 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
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 rateRNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing.
Burd C, Dreyfuss G. RNA binding specificity of hnRNP A1: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing. The EMBO Journal 1994, 13: 1197-204. PMID: 7510636, PMCID: PMC394929, DOI: 10.1002/j.1460-2075.1994.tb06369.x.Peer-Reviewed Original ResearchAnimalsBase SequenceBinding SitesCell NucleusConsensus SequenceDNA PrimersGlobinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsIntronsMolecular Sequence DataOligodeoxyribonucleotidesOligoribonucleotidesRecombinant ProteinsRibonucleoproteinsRNARNA PrecursorsRNA SplicingRNA-Binding ProteinsUltraviolet Rays
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