2005
Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae
Shih J, Reck-Peterson S, Newitt R, Mooseker M, Aebersold R, Herskowitz I. Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae. Molecular Biology Of The Cell 2005, 16: 4595-4608. PMID: 16030260, PMCID: PMC1237067, DOI: 10.1091/mbc.e05-02-0108.Peer-Reviewed Original ResearchConceptsCell polarityPolarity proteinsActin functionCell wall morphogenesisCell polarity proteinsYeast cell polarityPresumptive bud siteCell separation defectATP-sensitive mannerTandem mass spectrometry analysisNonessential proteinsWall morphogenesisMolecular functionsBud sitePolarized localizationSpa2pMass spectrometry analysisSite of growthSaccharomyces cerevisiaeMyo2pCoimmunoprecipitation strategyCell cycleF-actinIndirect interactionsProteinA 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
1999
An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contactRole of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization
Zhou D, Mooseker M, Galán J. Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization. Science 1999, 283: 2092-2095. PMID: 10092234, DOI: 10.1126/science.283.5410.2092.Peer-Reviewed Original Research
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
1994
Identification of a Divergent Actin-related Protein in Drosophila
Frankel S, Heintzelman M, Artavanis-Tsakonas S, Mooseker M. Identification of a Divergent Actin-related Protein in Drosophila. Journal Of Molecular Biology 1994, 235: 1351-1356. PMID: 8308899, DOI: 10.1006/jmbi.1994.1090.Peer-Reviewed Original ResearchConceptsActin-related proteinsAmino acid identityPrimary sequence homologyDivergent actinConventional actinPolytene chromosomesEarly embryogenesisAcid identityX chromosomeSequence homologyGenomic DNAOverall divergenceSequence insertionNew isotypeActinDrosophilaProteinEmbryogenesisChromosomesHomologyGenesStages of developmentTranscriptsUnique locationLater stagesDifferential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms
Fanning A, Wolenski J, Mooseker M, Izant J. Differential regulation of skeletal muscle myosin‐II and brush border myosin‐I enzymology and mechanochemistry by bacterially produced tropomyosin isoforms. Cytoskeleton 1994, 29: 29-45. PMID: 7820856, DOI: 10.1002/cm.970290104.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceAnimalsCa(2+) Mg(2+)-ATPaseCarrier ProteinsCell MovementChick EmbryoDNA, ComplementaryEscherichia coliIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMolecular WeightMuscle ProteinsMyosinsProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsSequence HomologySpecies SpecificityTropomyosinVertebratesXenopusConceptsAlpha-tropomyosinMuscle myosin IIMyosin enzymologyMyosin isoformsTwo- toStriated MuscleMgATPase activityDifferential regulationBrush border myosinDetectable effectIsoformsLow affinityChimeric tropomyosinsMuscle tropomyosinMuscle alpha-tropomyosinSkeletal muscle myosin IIActinTropomyosin isoformsMuscle myosinF-actin
1993
An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells.
Peterson M, Bement W, Mooseker M. An in vitro model for the analysis of intestinal brush border assembly. II. Changes in expression and localization of brush border proteins during cell contact-induced brush border assembly in Caco-2BBe cells. Journal Of Cell Science 1993, 105 ( Pt 2): 461-72. PMID: 8408277, DOI: 10.1242/jcs.105.2.461.Peer-Reviewed Original ResearchActinsAdenocarcinomaAmino Acid SequenceAnimalsBiomarkersBirdsCarrier ProteinsCattleCell CommunicationCell PolarityClone CellsColonic NeoplasmsCytoskeletonGene Expression Regulation, NeoplasticHumansIntestinal MucosaMicrofilament ProteinsMicrovilliMolecular Sequence DataMyosinsNeoplasm ProteinsOligo-1,6-GlucosidaseSequence AlignmentSequence Homology, Amino AcidSpecies SpecificitySucraseTumor Cells, CulturedCloning of a Secretory Gelsolin from Drosophila melanogaster
Heintzelman M, Frankel S, Artavanis-Tsakonas S, Mooseker M. Cloning of a Secretory Gelsolin from Drosophila melanogaster. Journal Of Molecular Biology 1993, 230: 709-716. PMID: 8386771, DOI: 10.1006/jmbi.1993.1191.Peer-Reviewed Original ResearchConceptsSecretory gelsolinAcid sequenceThird instar Drosophila larvaeDeduced amino acid sequenceFull-length complementary DNAInstar Drosophila larvaeClass of proteinsActin-binding proteinsAmino acid sequenceAmino acid residuesGelsolin sequenceThird chromosomeDrosophila melanogasterGelsolin familyCytoplasmic proteinsSignal peptideSingle geneDrosophila larvaeRepeat structureActin filamentsMonomeric actinAcid residuesBarbed endsPrimary structureNorthern blot
1992
Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation.
Schafer D, Mooseker M, Cooper J. Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation. Journal Of Cell Biology 1992, 118: 335-346. PMID: 1629237, PMCID: PMC2290044, DOI: 10.1083/jcb.118.2.335.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActinsAnimalsAntibodiesCells, CulturedChick EmbryoChickensCochleaDestrinElectrophoresis, Polyacrylamide GelEpithelial CellsEpitheliumFluorescent Antibody TechniqueIntestinesKidneyMacromolecular SubstancesMicrofilament ProteinsMicrovilliMusclesPigment Epithelium of EyeSubcellular FractionsConceptsIntestinal epithelial cellsNuclei of cellsBiochemical fractionationJunctional complexesActin filamentsCell-cell junctional complexesSingle intestinal epithelial cellsBarbed endsEpithelial cellsSensory epitheliumCell-cell contactIntact intestinal epithelial cellsAffinity-purified polyclonal antibodiesProtein bindsCapping proteinIntestinal epitheliumZonula adherensCell junctionsChick embryo kidney cellsPattern coincidentEmbryo kidney cellsProteinConfocal microscopyKidney cellsIsolated intestinal epithelial cells
1990
Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo
Heintzelman M, Mooseker M. Structural and compositional analysis of early stages in microvillus assembly in the enterocyte of the chick embryo. Differentiation 1990, 43: 175-182. PMID: 2387484, DOI: 10.1111/j.1432-0436.1990.tb00444.x.Peer-Reviewed Original ResearchAssembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine
Heintzelman M, Mooseker M. Assembly of the brush border cytoskeleton: Changes in the distribution of microvillar core proteins during enterocyte differentiation in adult chicken intestine. Cytoskeleton 1990, 15: 12-22. PMID: 2403846, DOI: 10.1002/cm.970150104.Peer-Reviewed Original Research
1988
Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms
West A, Isaac C, Carboni J, Morrow J, Mooseker M, Barwick K. Localization of villin, a cytoskeletal protein specific to microvilli, in human ileum and colon and in colonic neoplasms. Gastroenterology 1988, 94: 343-352. PMID: 3335311, DOI: 10.1016/0016-5085(88)90421-0.Peer-Reviewed Original ResearchCharacterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin
Alicea H, Mooseker M. Characterization of villin from the intestinal brush border of the rat, and comparative analysis with avian villin. Cytoskeleton 1988, 9: 60-72. PMID: 3356045, DOI: 10.1002/cm.970090107.Peer-Reviewed Original ResearchA domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin
Petrucci T, Mooseker M, Morrow J. A domain of synapsin I involved with actin bundling shares immunologic cross‐reactivity with villin. Journal Of Cellular Biochemistry 1988, 36: 25-35. PMID: 3125185, DOI: 10.1002/jcb.240360104.Peer-Reviewed Original ResearchConceptsBovine synapsin ISynapsin IActin binding proteinsPeptide mappingTwo-dimensional peptide mapsSmall synaptic vesiclesPhosphorylation controlBundling proteinActin bindingUnrelated proteinsActin bundlesActin filamentsNeuronal phosphoproteinSynapsin I.Binding proteinVivo roleSynaptic vesiclesParent proteinProteinPeptide mapsChymotryptic digestionVillinPeptide fragmentsCross reactFragments
1987
Assembly 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 ResearchNucleation of actin polymerization by villin and elongation at subcritical monomer concentration.
Weber A, Northrop J, Bishop M, Ferrone F, Mooseker M. Nucleation of actin polymerization by villin and elongation at subcritical monomer concentration. Biochemistry 1987, 26: 2528-36. PMID: 3607030, DOI: 10.1021/bi00383a019.Peer-Reviewed Original ResearchKinetics of actin elongation and depolymerization at the pointed end.
Weber A, Northrop J, Bishop M, Ferrone F, Mooseker M. Kinetics of actin elongation and depolymerization at the pointed end. Biochemistry 1987, 26: 2537-44. PMID: 3607031, DOI: 10.1021/bi00383a020.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 proteinsMicrovilliDifferent calcium dependence of the capping and cutting activities of villin.
Northrop J, Weber A, Mooseker M, Franzini-Armstrong C, Bishop M, Dubyak G, Tucker M, Walsh T. Different calcium dependence of the capping and cutting activities of villin. Journal Of Biological Chemistry 1986, 261: 9274-9281. PMID: 3087992, DOI: 10.1016/s0021-9258(18)67650-1.Peer-Reviewed Original Research