2007
Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis. FEBS Letters 2007, 581: 644-650. PMID: 17257598, PMCID: PMC1861834, DOI: 10.1016/j.febslet.2007.01.021.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsEndocytosisHeLa CellsHumansImmunoprecipitationMiceMyosin Type INerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingProtein TransportRatsSrc Homology DomainsSynapsesTissue ExtractsTransferrinTwo-Hybrid System TechniquesConceptsSH3 domainMyosin 1eSynaptojanin 1Myosin IIntact SH3 domainDominant-negative mannerReceptor-mediated endocytosisHigher eukaryotesArp2/3 complexInhibits endocytosisPlasma membraneActin polymerizationImportant regulatorEndocytosisHuman class IProminent functionDynaminTail regionDomainEukaryotesClathrinYeastRegulatorProteinBinds
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 interactionsProtein
2003
Myosin-Va Binds to and Mechanochemically Couples Microtubules to Actin Filaments
Cao T, Chang W, Masters S, Mooseker M. Myosin-Va Binds to and Mechanochemically Couples Microtubules to Actin Filaments. Molecular Biology Of The Cell 2003, 15: 151-161. PMID: 14565972, PMCID: PMC307536, DOI: 10.1091/mbc.e03-07-0504.Peer-Reviewed Original Research
2001
The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin
Wang Y, Miller A, Mooseker M, Koleske A. The Abl-related gene (Arg) nonreceptor tyrosine kinase uses two F-actin-binding domains to bundle F-actin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14865-14870. PMID: 11752434, PMCID: PMC64950, DOI: 10.1073/pnas.251249298.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAnimalsMiceMicroscopy, ElectronProtein BindingProtein-Tyrosine KinasesRecombinant Fusion ProteinsConceptsF-actin-binding domainActin-rich structuresAbl family kinasesNonreceptor tyrosine kinaseF-actinActin cytoskeletonFamily kinasesFluorescent protein fusion proteinTyrosine kinaseActin-bundling activityProtein fusion proteinActin cytoskeletal structuresCellular morphogenesisSwiss 3T3 fibroblastsBundling activityDeletion mutantsCytoskeletal structuresC-terminusFusion proteinFunctional interactionKinaseActin moleculesCytoskeletonPositive cooperativityArgHigh Affinity Binding of Brain Myosin-Va to F-actin Induced by Calcium in the Presence of ATP*
Tauhata S, dos Santos D, Taylor E, Mooseker M, Larson R. High Affinity Binding of Brain Myosin-Va to F-actin Induced by Calcium in the Presence of ATP*. Journal Of Biological Chemistry 2001, 276: 39812-39818. PMID: 11517216, DOI: 10.1074/jbc.m102583200.Peer-Reviewed Original ResearchThe Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors
Reck-Peterson S, Tyska M, Novick P, Mooseker M. The Yeast Class V Myosins, Myo2p and Myo4p, Are Nonprocessive Actin-Based Motors. Journal Of Cell Biology 2001, 153: 1121-1126. PMID: 11381095, PMCID: PMC2174330, DOI: 10.1083/jcb.153.5.1121.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAnimalsAntibodiesBrainCalciumCalmodulin-Binding ProteinsCarrier ProteinsChickensFungal ProteinsKineticsMicroscopy, VideoMolecular Motor ProteinsMovementMyosin Heavy ChainsMyosin Type IIMyosin Type VMyosinsNerve Tissue ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe Proteins
2000
The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN
Espindola F, Suter D, Partata L, Cao T, Wolenski J, Cheney R, King S, Mooseker M. The light chain composition of chicken brain myosin‐Va: Calmodulin, myosin‐II essential light chains, and 8‐kDa dynein light chain/PIN. Cytoskeleton 2000, 47: 269-281. PMID: 11093248, DOI: 10.1002/1097-0169(200012)47:4<269::aid-cm2>3.0.co;2-g.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsBrainCalmodulinCalpainCarrier ProteinsCells, CulturedChick EmbryoChickensDrosophila ProteinsDyneinsElectrophoresis, Polyacrylamide GelFlagellaGanglia, SpinalImmunoglobulin GIntermediate Filament ProteinsMiceMicroscopy, FluorescenceMolecular Sequence DataMyosin Heavy ChainsMyosin Light ChainsMyosin Type VMyosinsNeuronsProtein BindingProtein Structure, TertiarySequence Analysis, Protein
1998
Human myosin-IXb is a mechanochemically active motor and a GAP for rho
Post P, Bokoch G, Mooseker M. Human myosin-IXb is a mechanochemically active motor and a GAP for rho. Journal Of Cell Science 1998, 111: 941-950. PMID: 9490638, DOI: 10.1242/jcs.111.7.941.Peer-Reviewed Original ResearchActinsAdenosine TriphosphateAlternative SplicingAmino Acid SequenceAnimalsCalciumCalmodulinGTP PhosphohydrolasesGTPase-Activating ProteinsGTP-Binding ProteinsHumansLeukocytesMolecular Sequence DataMuscle ContractionMyosinsProtein BindingProteinsRas GTPase-Activating ProteinsRas ProteinsRatsRho GTP-Binding Proteins
1994
Multiple unconventional myosin domains of the intestinal brush border cytoskeleton
Heintzelman M, Hasson T, Mooseker M. Multiple unconventional myosin domains of the intestinal brush border cytoskeleton. Journal Of Cell Science 1994, 107: 3535-3543. PMID: 7706404, DOI: 10.1242/jcs.107.12.3535.Peer-Reviewed Original ResearchDifferential 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
1990
Binding of brush border myosin I to phospholipid vesicles.
Hayden S, Wolenski J, Mooseker M. Binding of brush border myosin I to phospholipid vesicles. Journal Of Cell Biology 1990, 111: 443-451. PMID: 2143194, PMCID: PMC2116197, DOI: 10.1083/jcb.111.2.443.Peer-Reviewed Original ResearchConceptsBB myosin IMyosin IBrush border myosin IMyosin I heavy chainMembrane-binding domainActin filament corePhospholipid vesiclesATP-sensitive mannerPlasma membraneIntestinal epithelial cellsF-actinMembrane interactionsPhosphatidylglycerol vesiclesFree proteinCOOH-terminalAnionic phospholipidsImmunoblot analysisVesiclesEpithelial cellsImmunoblot stainingM. SimilarHeavy chainActinStructural informationNeutral phospholipids
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 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
1985
Role of myosin in terminal web contraction in isolated intestinal epithelial brush borders.
Keller T, Conzelman K, Chasan R, Mooseker M. Role of myosin in terminal web contraction in isolated intestinal epithelial brush borders. Journal Of Cell Biology 1985, 100: 1647-1655. PMID: 3988804, PMCID: PMC2113869, DOI: 10.1083/jcb.100.5.1647.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsChickensIntestinal MucosaMicrovilliMyosinsPhosphorylationProtein BindingSolubility
1984
Studies on the spectrin-like protein from the intestinal brush border, TW 260/240, and characterization of its interaction with the cytoskeleton and actin.
Pearl M, Fishkind D, Mooseker M, Keene D, Keller T. Studies on the spectrin-like protein from the intestinal brush border, TW 260/240, and characterization of its interaction with the cytoskeleton and actin. Journal Of Cell Biology 1984, 98: 66-78. PMID: 6538573, PMCID: PMC2112984, DOI: 10.1083/jcb.98.1.66.Peer-Reviewed Original Research
1983
Effects of villin on the polymerization and subunit exchange of actin
Wang Y, Bonder E, Mooseker M, Taylor D. Effects of villin on the polymerization and subunit exchange of actin. Cytoskeleton 1983, 3: 151-165. PMID: 6883468, DOI: 10.1002/cm.970030205.Peer-Reviewed Original Research
1980
Brush-border calmodulin. A major component of the isolated microvillus core.
Howe C, Mooseker M, Graves T. Brush-border calmodulin. A major component of the isolated microvillus core. Journal Of Cell Biology 1980, 85: 916-923. PMID: 6893051, PMCID: PMC2111444, DOI: 10.1083/jcb.85.3.916.Peer-Reviewed Original Research
1971
Actin in the Brush-Border of Epithelial Cells of the Chicken Intestine
Tilney L, Mooseker M. Actin in the Brush-Border of Epithelial Cells of the Chicken Intestine. Proceedings Of The National Academy Of Sciences Of The United States Of America 1971, 68: 2611-2615. PMID: 4944636, PMCID: PMC389479, DOI: 10.1073/pnas.68.10.2611.Peer-Reviewed Original Research