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
1992
Characterization of the enterocyte-like brush border cytoskeleton of the C2BBe clones of the human intestinal cell line, Caco-2
Peterson M, Mooseker M. Characterization of the enterocyte-like brush border cytoskeleton of the C2BBe clones of the human intestinal cell line, Caco-2. Journal Of Cell Science 1992, 102: 581-600. PMID: 1506435, DOI: 10.1242/jcs.102.3.581.Peer-Reviewed Original ResearchConceptsMyosin IBB myosin IC2BBe cellsATP-dependent associationBrush border cytoskeletonApical brush borderHeavy chainDomain-specific monoclonal antibodiesBrush borderFilter-grown monolayersCaco-2Cell line Caco-2Human colonic epithelial cellsHuman intestinal cell lineMyosin I.Myosin IIIntestinal cell linePhysical associationLaser scanning confocal microscopyProtein villinCytoskeletonCell culture modelCell typesPattern of distributionVivo structureThe molecular architecture of an insect midgut brush border cytoskeleton.
Bonfanti P, Colombo A, Heintzelman M, Mooseker M, Camatini M. The molecular architecture of an insect midgut brush border cytoskeleton. European Journal Of Cell Biology 1992, 57: 298-307. PMID: 1511705.Peer-Reviewed Original ResearchConceptsTwo-dimensional gel analysisMolecular architectureMultiple isoelectric variantsBrush border cytoskeletonLepidopteran larvaeBB myosin IVertebrate intestineBrush borderMyosin IOrganelle exclusionHeavy meromyosin decorationCytoskeletal apparatusMyosin IINonmuscle cellsActin filamentsCytoskeletonIsoelectric variantsGel analysisInstar larvaeMajor isoformsStructural organizationRhodamine phalloidinCore proteinIntestinal brush borderMidgut
1991
Chapter 3 Structural and Functional Dissection of a Membrane-Bound Mechanoenzyme: Brush Border Myosin I
Mooseker M, Wolenski J, Coleman T, Hayden S, Cheney R, Espreafico E, Heintzelman M, Peterson M. Chapter 3 Structural and Functional Dissection of a Membrane-Bound Mechanoenzyme: Brush Border Myosin I. Current Topics In Membranes 1991, 38: 31-55. DOI: 10.1016/s0070-2161(08)60780-7.Peer-Reviewed Original ResearchBrush border myosin IBB myosin IMyosin ICalmodulin light chainsMicrovillar membraneProtein domain structureHeavy chainFunctional dissectionLight chainLinker proteinActin bindingMyosin I.Intestinal epithelial cellsActin filamentsMV membranePrimary structureApical membraneAcidic phospholipidsSubunit compositionTerminal webGlycoprotein bindsEpithelial cells
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