2008
Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells
Stabach PR, Devarajan P, Stankewich MC, Bannykh S, Morrow JS. Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells. American Journal Of Physiology - Cell Physiology 2008, 295: c1202-c1214. PMID: 18768923, PMCID: PMC2584975, DOI: 10.1152/ajpcell.00273.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnkyrin RepeatAnkyrinsCell PolarityChlorocebus aethiopsCOS CellsCytoplasmDogsEndoplasmic ReticulumGolgi ApparatusHumansMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein ConformationProtein FoldingProtein Sorting SignalsProtein TransportRatsRecombinant Fusion ProteinsRNA InterferenceRNA, Small InterferingSodium-Potassium-Exchanging ATPaseTime FactorsTransfectionViral Envelope ProteinsConceptsEndoplasmic reticulumSecretory pathwayPlasma membraneVesicular stomatitis virus G proteinMadin-Darby canine kidney cellsVirus G proteinSmall hairpin RNACanine kidney cellsGolgi traffickingAnkyrin RGolgi transportSemipermeabilized cellsER retentionCytoplasmic domainMembrane proteinsAssembly pathwayProtein ankyrinIntracellular traffickingAnkyrinFusion proteinSimilar phenotypeG proteinsSuch phenotypesHairpin RNACultured cells
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
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 distribution