2013
Competing molecular interactions of aPKC isoforms regulate neuronal polarity
Parker SS, Mandell EK, Hapak SM, Maskaykina IY, Kusne Y, Kim JY, Moy JK, St. John PA, Wilson JM, Gothard KM, Price TJ, Ghosh S. Competing molecular interactions of aPKC isoforms regulate neuronal polarity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 14450-14455. PMID: 23940317, PMCID: PMC3761571, DOI: 10.1073/pnas.1301588110.Peer-Reviewed Original ResearchConceptsAtypical protein kinase CNeuronal polarityAPKC isoformsProtein kinase CCell polarityPolarized neuronsAlternative transcriptsKinase CPar3Supernumerary axonsIsoformsEmbryonic hippocampal neuronsMolecular interactionsOverexpressionPresumptive axonsMolecular modelHippocampal neuronsPolarityPKMTranscriptsRegulatorIntermolecular competitionInteractsNeuronsDisruptsAutophagy is differentially induced in prostate cancer LNCaP, DU145 and PC-3 cells via distinct splicing profiles of ATG5
Ouyang DY, Xu LH, He XH, Zhang YT, Zeng LH, Cai JY, Ren S. Autophagy is differentially induced in prostate cancer LNCaP, DU145 and PC-3 cells via distinct splicing profiles of ATG5. Autophagy 2013, 9: 20-32. PMID: 23075929, PMCID: PMC3542215, DOI: 10.4161/auto.22397.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlternative SplicingAutophagyAutophagy-Related Protein 12Autophagy-Related Protein 5Base SequenceCell Line, TumorGene Knockdown TechniquesHumansMaleMicrotubule-Associated ProteinsProstatic NeoplasmsRNA, NeoplasmSequestosome-1 ProteinSmall Ubiquitin-Related Modifier ProteinsTransfectionValproic AcidConceptsATG12-ATG5 conjugatePC-3 cellsDU145 cellsAutophagic responseProstate cancer cellsLC3 punctaFull-length ATG5Autophagy-related proteinsCancer cellsCell linesDifferent prostate cancer cellsDefects of autophagyKnockdown of ATG5Conversion of LC3Splicing profilesAutophagy adaptorsAlternative transcriptsLC3-II conjugatesAutophagic stimulationAutophagy pathwayProstate cancer LNCaPAutophagy inductionATG5 geneSQSTM1 proteinCanonical transcripts
2004
The Appearance of a Protein Kinase A-regulated Splice Isoform of slo Is Associated with the Maturation of Neurons That Control Reproductive Behavior*
Zhang Y, Joiner WJ, Bhattacharjee A, Rassendren F, Magoski NS, Kaczmarek LK. The Appearance of a Protein Kinase A-regulated Splice Isoform of slo Is Associated with the Maturation of Neurons That Control Reproductive Behavior*. Journal Of Biological Chemistry 2004, 279: 52324-52330. PMID: 15375169, DOI: 10.1074/jbc.m408543200.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsAplysiaCell DifferentiationCHO CellsCricetinaeCyclic AMP-Dependent Protein KinasesDNA, ComplementaryIn Vitro TechniquesLarge-Conductance Calcium-Activated Potassium ChannelsMolecular Sequence DataNeuronsPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedProtein IsoformsRecombinant ProteinsReproductionConceptsBag cell neuronsReproductive behaviorSlo geneConsensus phosphorylation sitesCell cDNA libraryProtein kinase ACell neuronsChinese hamster ovary cellsPhosphorylation sitesCatalytic subunitHamster ovary cellsAlternative transcriptsCDNA librarySplice isoformsKinase ABK channel activityMaturation of neuronsPKA inhibitorVoltage-dependent channelsOvary cellsBrief synaptic stimulationChannel activityMature neuronsIsoformsPKA
2002
A Novel Gene Encoding a TIG Multiple Domain Protein Is a Positional Candidate for Autosomal Recessive Polycystic Kidney Disease
Xiong H, Chen Y, Yi Y, Tsuchiya K, Moeckel G, Cheung J, Liang D, Tham K, Xu X, Chen XZ, Pei Y, Zhao ZJ, Wu G. A Novel Gene Encoding a TIG Multiple Domain Protein Is a Positional Candidate for Autosomal Recessive Polycystic Kidney Disease. Genomics 2002, 80: 96-104. PMID: 12079288, DOI: 10.1006/geno.2002.6802.Peer-Reviewed Original ResearchConceptsNorthern blot analysisNovel genesGenetic intervalStrong positional candidate geneMultiple alternative transcriptsExpression of PKHD1Positional candidate genesAutosomal recessive polycystic kidney diseaseBlot analysisImmunoglobulin-like foldGenetic linkage analysisTIG domainMultiple-domain proteinsDomain proteinsSitu hybridization analysisGenomic regionsPolycystic kidney diseaseAlternative transcriptsPositional candidatesRecessive polycystic kidney diseaseCommon hereditary renal cystic diseasesHepatic disease 1Gene productsCloning strategyCandidate genes
1999
Brain and Muscle Express a Unique Alternative Transcript of αΙΙ Spectrin †
Cianci C, Zhang Z, Pradhan D, Morrow J. Brain and Muscle Express a Unique Alternative Transcript of αΙΙ Spectrin †. Biochemistry 1999, 38: 15721-15730. PMID: 10625438, DOI: 10.1021/bi991458k.Peer-Reviewed Original ResearchConceptsAlternative mRNA splicingMRNA splicingAlphaII-spectrinBp insertionNovel protein interaction siteEmbryonic tissuesInsert 2Alternative exon usageProtein interaction sitesAmino acid sequenceDifferent splice formsAmino acid insertionMouse embryonic tissuesInsert-1Amino acid substitutionsSkeletal muscleGene familyDynamic molecular modelingMature proteinUnanticipated functionAlternative splicingExon usageIndividual transcriptsAlternative transcriptsSplice forms
1998
Alternative splicing of rearranged T cell receptor δ sequences to the constant region of the α locus
Livák F, Schatz D. Alternative splicing of rearranged T cell receptor δ sequences to the constant region of the α locus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 5694-5699. PMID: 9576946, PMCID: PMC20441, DOI: 10.1073/pnas.95.10.5694.Peer-Reviewed Original ResearchConceptsCalpha geneTCRalpha/delta locusT cell receptor alpha/delta locusDelta locusAlpha/delta locusProtein coding capacityTranscriptional controlAlternative splicingSplicing variationsDistinct functional capacitiesAlternative transcriptsDelta proteinΑ locusChimeric proteinConstant genesAlpha proteinGene-deficient miceCoding capacityGenesThymocyte developmentAlphabeta thymocytesNovel insightsTCRbeta chainLociDistinct diversity
1996
The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle.
Weed SA, Stabach PR, Oyer CE, Gallagher PG, Morrow JS. The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle. Laboratory Investigation 1996, 74: 1117-29. PMID: 8667615.Peer-Reviewed Original ResearchConceptsBeta ISpectrin skeletonSkeletal muscleMost such mutationsGene transferAdult mouse skeletal muscleDominant-negative fashionErythroid lineage cellsNeonatal skeletal muscleCultured muscle cellsAlpha beta heterodimersErythrocyte shape abnormalitiesMuscle cellsMouse skeletal muscleDefective proteinSpectrin geneAlternative transcriptsHemolytic phenotypeCDNA constructsNull phenotypeC2C12 myoblastsBeta heterodimerSpectrin mutationsSedimentation velocity analysisIntracellular distributionIdentification 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
1993
The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons.
Malchiodi-Albedi F, Ceccarini M, Winkelmann J, Morrow J, Petrucci T. The 270 kDa splice variant of erythrocyte beta-spectrin (beta I sigma 2) segregates in vivo and in vitro to specific domains of cerebellar neurons. Journal Of Cell Science 1993, 106 ( Pt 1): 67-78. PMID: 8270644, DOI: 10.1242/jcs.106.1.67.Peer-Reviewed Original ResearchConceptsBeta IPostsynaptic densityMultiple alternative transcriptsBeta-spectrin isoformBeta-spectrin genePlasma membrane stainingAlpha beta heterodimersNon-erythroid alpha-spectrinRegion of alphaCerebellar granule cellsDistinct genesPrecise segregationSubstantial homologyBiochemical restrictionsSingle protein bandAlternative transcriptsDistinct cytoplasmicUnique sequencesCerebellar neuronsSpectrin isoformsBeta heterodimerAlpha-spectrinSpectrin complexSplice variantsTargeting mechanism
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