2005
A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis
Osterweil E, Wells D, Mooseker M. A role for myosin VI in postsynaptic structure and glutamate receptor endocytosis. Journal Of Cell Biology 2005, 168: 329-338. PMID: 15657400, PMCID: PMC2171578, DOI: 10.1083/jcb.200410091.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdenosine TriphosphateAlpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidAnimalsAstrocytesBrainBrain ChemistryDendritesDendritic SpinesDiscs Large Homolog 1 ProteinDyneinsEndocytosisFemaleGlial Fibrillary Acidic ProteinGuanylate KinasesInsulinMaleMembrane ProteinsMiceMice, Inbred C57BLMice, Mutant StrainsMicrofilament ProteinsMicroscopy, ElectronMyosin Heavy ChainsMyosin VIIaMyosinsNerve Tissue ProteinsNeuronsReceptors, AMPAReceptors, GlutamateSucroseSynapsesSynaptic MembranesSynaptosomesTransferrinConceptsHippocampal neuronsDendritic spinesIsoxazole propionic acid-type glutamate receptorsWild-type hippocampal neuronsShort dendritic spinesNumber of synapsesSynapse lossNeurons displaySynapse numberGlutamate receptorsNervous systemNonneuronal cellsPostsynaptic structuresSynaptic structurePostsynaptic densityDominant negative disruptionSignificant deficitsAstrogliosisNeuronsBrainMYO6SpineSynapsesReceptor endocytosisMyosin VI
1997
Actin-binding membrane proteins identified by F-actin blot overlays.
Luna E, Pestonjamasp K, Cheney R, Strassel C, Lu T, Chia C, Hitt A, Fechheimer M, Furthmayr H, Mooseker M. Actin-binding membrane proteins identified by F-actin blot overlays. Society Of General Physiologists Series 1997, 52: 3-18. PMID: 9210216.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAmino Acid SequenceAnimalsBlotting, WesternBrainBreast NeoplasmsCattleChick EmbryoDictyosteliumElectrophoresis, Polyacrylamide GelHeLa CellsHumansIodine RadioisotopesMammalsMembrane ProteinsMiceMicrofilament ProteinsNeuroblastomaNeuropeptidesNeutrophilsSodium Dodecyl SulfateTumor Cells, CulturedConceptsBlot overlayApparent molecular massMembrane proteinsF-actinF-actin binding proteinMolecular massControl cell shapePeripheral membrane proteinsSpecialized membrane domainsCell-cell adhesionPlasma membrane-enriched fractionActin-binding proteinsMammalian cell linesCell surface extensionsMembrane-enriched fractionMembrane rufflesProtein 4.1Membrane domainsMammalian cellsDictyostelium discoideumSoil amoebaPseudopod dynamicsCell shapeEfficient chemotaxisMembrane bilayer
1989
Phosphorylation of the tight-junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance
Stevenson B, Anderson J, Braun I, Mooseker M. Phosphorylation of the tight-junction protein ZO-1 in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Biochemical Journal 1989, 263: 597-599. PMID: 2597123, PMCID: PMC1133468, DOI: 10.1042/bj2630597.Peer-Reviewed Original ResearchZO-1 and cingulin: tight junction proteins with distinct identities and localizations
Stevenson B, Heintzelman M, Anderson J, Citi S, Mooseker M. ZO-1 and cingulin: tight junction proteins with distinct identities and localizations. American Journal Of Physiology 1989, 257: c621-c628. PMID: 2679124, DOI: 10.1152/ajpcell.1989.257.4.c621.Peer-Reviewed Original ResearchConceptsCell-cell contactPlasma membraneHepatoma tissue cultureZO-1MDCK cellsMadin-Darby canine kidney cellsCanine kidney cellsSubconfluent MDCK cellsSingle polypeptideCingulinHepatoma cell lineMolecular massChicken small intestineDistinct localizationImmunoblot analysisJunctional membranesImmunofluorescent localizationCell linesKidney cellsJunction proteinsKidney distalTight junctionsChicken intestineConfluent monolayersProteinZO-1 mRNA and protein expression during tight junction assembly in Caco-2 cells.
Anderson J, Van Itallie C, Peterson M, Stevenson B, Carew E, Mooseker M. ZO-1 mRNA and protein expression during tight junction assembly in Caco-2 cells. Journal Of Cell Biology 1989, 109: 1047-1056. PMID: 2670954, PMCID: PMC2115763, DOI: 10.1083/jcb.109.3.1047.Peer-Reviewed Original ResearchHepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis.
Anderson J, Glade J, Stevenson B, Boyer J, Mooseker M. Hepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis. American Journal Of Pathology 1989, 134: 1055-62. PMID: 2719075, PMCID: PMC1879891.Peer-Reviewed Original ResearchConceptsZO-1 proteinZO-1Tight junctionsConsecutive daily subcutaneous injectionsFrozen sectionsReflux of bileDaily subcutaneous injectionsBile duct obstructionCommon bile ductMale Sprague-DawleyHepatocyte tight junctionsBile duct ligation resultsTight junction protein ZO-1Cholestatic modelsDuct obstructionBile ductSubcutaneous injectionCholestatic liverRat modelEthinyl estradiolSprague-DawleyProtein ZO-1Immunoperoxidase stainingZO-1 stainingImmunohistochemical localizationContributions of the β‐subunit to spectrin structure and function
Coleman T, Fishkind D, Mooseker M, Morrow J. Contributions of the β‐subunit to spectrin structure and function. Cytoskeleton 1989, 12: 248-263. PMID: 2524283, DOI: 10.1002/cm.970120406.Peer-Reviewed Original Research
1988
Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance.
Stevenson B, Anderson J, Goodenough D, Mooseker M. Tight junction structure and ZO-1 content are identical in two strains of Madin-Darby canine kidney cells which differ in transepithelial resistance. Journal Of Cell Biology 1988, 107: 2401-2408. PMID: 3058723, PMCID: PMC2115690, DOI: 10.1083/jcb.107.6.2401.Peer-Reviewed Original ResearchCharacterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells.
Anderson J, Stevenson B, Jesaitis L, Goodenough D, Mooseker M. Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. Journal Of Cell Biology 1988, 106: 1141-1149. PMID: 2452168, PMCID: PMC2115004, DOI: 10.1083/jcb.106.4.1141.Peer-Reviewed Original Research
1987
Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.
Mische S, Mooseker M, Morrow J. Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding. Journal Of Cell Biology 1987, 105: 2837-2845. PMID: 3693401, PMCID: PMC2114693, DOI: 10.1083/jcb.105.6.2837.Peer-Reviewed Original ResearchAssembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes.
Shibayama T, Carboni J, Mooseker M. Assembly of the intestinal brush border: appearance and redistribution of microvillar core proteins in developing chick enterocytes. Journal Of Cell Biology 1987, 105: 335-344. PMID: 2956268, PMCID: PMC2114914, DOI: 10.1083/jcb.105.1.335.Peer-Reviewed Original ResearchBeta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions.
Coleman T, Harris A, Mische S, Mooseker M, Morrow J. Beta spectrin bestows protein 4.1 sensitivity on spectrin-actin interactions. Journal Of Cell Biology 1987, 104: 519-526. PMID: 3818791, PMCID: PMC2114562, DOI: 10.1083/jcb.104.3.519.Peer-Reviewed Original Research
1986
Cytoskeletal proteins of the rat kidney proximal tubule brush border.
Rodman J, Mooseker M, Farquhar M. Cytoskeletal proteins of the rat kidney proximal tubule brush border. European Journal Of Cell Biology 1986, 42: 319-27. PMID: 3545840.Peer-Reviewed Original ResearchConceptsProximal tubule cellsBrush borderIntestinal brush borderTubule cellsProximal tubule brush borderKidney proximal tubule cellsTubule brush borderRat kidney proximal tubule cellsTerminal web regionKidney brush borderTerminal webImmunogold labeling procedureKidneyCell typesImmunoelectron microscopyBasolateral membraneCytoskeletal componentsVillinCytoskeletal proteinsMicrovilli
1985
Organization, Chemistry, and Assembly of the Cytoskeletal Apparatus of the Intestinal Brush Border
Mooseker M. Organization, Chemistry, and Assembly of the Cytoskeletal Apparatus of the Intestinal Brush Border. Annual Review Of Cell And Developmental Biology 1985, 1: 209-241. PMID: 3916317, DOI: 10.1146/annurev.cb.01.110185.001233.Peer-Reviewed Original ResearchMechanisms of cytoskeletal regulation: modulation of membrane affinity in avian brush border and erythrocyte spectrins.
Howe C, Sacramone L, Mooseker M, Morrow J. Mechanisms of cytoskeletal regulation: modulation of membrane affinity in avian brush border and erythrocyte spectrins. Journal Of Cell Biology 1985, 101: 1379-1385. PMID: 2931438, PMCID: PMC2113910, DOI: 10.1083/jcb.101.4.1379.Peer-Reviewed Original Research
1984
Brush border cytoskeleton and integration of cellular functions.
Mooseker M, Bonder E, Conzelman K, Fishkind D, Howe C, Keller T. Brush border cytoskeleton and integration of cellular functions. Journal Of Cell Biology 1984, 99: 104s-112s. PMID: 6378918, PMCID: PMC2275581, DOI: 10.1083/jcb.99.1.104s.Peer-Reviewed Original Research
1983
Actin binding proteins of the brush border
Mooseker M. Actin binding proteins of the brush border. Cell 1983, 35: 11-13. PMID: 6313218, DOI: 10.1016/0092-8674(83)90202-7.Peer-Reviewed Original ResearchCharacterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells.
Howe C, Mooseker M. Characterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells. Journal Of Cell Biology 1983, 97: 974-985. PMID: 6311843, PMCID: PMC2112603, DOI: 10.1083/jcb.97.4.974.Peer-Reviewed Original Research