2006
A limited number of genes are involved in the differentiation of germinal center B cells
Nakayama Y, Stabach P, Maher SE, Mahajan MC, Masiar P, Liao C, Zhang X, Ye Z, Tuck D, Bothwell AL, Newburger PE, Weissman SM. A limited number of genes are involved in the differentiation of germinal center B cells. Journal Of Cellular Biochemistry 2006, 99: 1308-1325. PMID: 16795035, DOI: 10.1002/jcb.20952.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsB-LymphocytesCell DifferentiationCell LineChildChild, PreschoolDithiothreitolDNA-Binding ProteinsGene Expression ProfilingGerminal CenterHumansMolecular Sequence DataNuclear ProteinsOligonucleotide Array Sequence AnalysisPalatine TonsilProtein FoldingRegulatory Factor X Transcription FactorsTranscription FactorsTunicamycinX-Box Binding Protein 1ConceptsUnfolded protein responseX-box binding protein 1Interferon regulatory factor 4Protein 1B lymphocyte-induced maturation protein-1Transcription factor B lymphocyte-induced maturation protein-1Post-transcriptional changesBinding protein 1Maturation protein-1Mature B cellsDisulfide isomeraseTranscription factorsLevel of expressionPlasmacytoma cell lineProtein responseGene expressionRegulatory factor 4GenesGerminal center B cellsLymphoblastoid cellsLimited inductionCell linesB cellsFactor 4Germinal center centroblastsHuman Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat
Stankewich MC, Stabach PR, Morrow JS. Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat. Journal Of Cell Science 2006, 119: 958-969. PMID: 16495487, DOI: 10.1242/jcs.02751.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCarrier ProteinsCell LineCells, CulturedChlorocebus aethiopsCloning, MolecularCOP-Coated VesiclesCOS CellsExonsGene Expression RegulationHumansMolecular Sequence DataPhosphoproteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentVesicular Transport ProteinsConceptsCOPII coatProline-rich C-terminal regionEndoplasmic reticulumTerminal proline-rich regionCOPII vesicle coatVesicular tubular clustersProline-rich regionWD repeat domainFull-length proteinAlternative mRNA splicingN-terminal domainC-terminal regionVesicle coatWD repeatsMammalian orthologuesVesicular trafficSecretory pathwayMRNA splicingExon utilizationExon 13Sec31pChromosome 10q24Gene productsSec31BSpecialized functions
1998
ADP 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 fractionsProteinPtdInsP2
1997
Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells
Devarajan P, Stabach P, De Matteis M, Morrow J. Na,K-ATPase transport from endoplasmic reticulum to Golgi requires the Golgi spectrin–ankyrin G119 skeleton in Madin Darby canine kidney cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 10711-10716. PMID: 9380700, PMCID: PMC23456, DOI: 10.1073/pnas.94.20.10711.Peer-Reviewed Original ResearchConceptsMembrane proteinsEndoplasmic reticulumSpectrin skeletonVesicular tubular clustersActin-binding domainSpecific membrane proteinsMadin-Darby canine kidney cellsK-ATPase transportCanine kidney cellsDynactin complexVesicle traffickingCargo proteinsGolgi spectrinTrafficking systemBeta-COPMembrane compartmentsTransport of alphaAdapter proteinCis-GolgiGolgi membranesGolgi stacksDocking complexBetaI spectrinGolgiBeta NA
1996
Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta I sigma spectrin and associates with the Golgi apparatus.
Devarajan P, Stabach PR, Mann AS, Ardito T, Kashgarian M, Morrow JS. Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta I sigma spectrin and associates with the Golgi apparatus. Journal Of Cell Biology 1996, 133: 819-830. PMID: 8666667, PMCID: PMC2120834, DOI: 10.1083/jcb.133.4.819.Peer-Reviewed Original ResearchConceptsMDCK cell lysatesGolgi apparatusMDCK cellsBeta IDomain IPlasma membrane localizationTrans-Golgi networkPutative regulatory domainCell lysatesPolarized vesicle transportMembrane-associated proteinsCell cycle controlSubset of endosomesNovel ankyrinPolarity developmentVesicle transportMotif characteristicMembrane localizationRegulatory domainProtein microdomainsSequence comparisonAlternative transcriptsRepetitive domainSubconfluent MDCK cellsMembrane skeleton