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
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