2000
Compartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast
Barral Y, Mermall V, Mooseker M, Snyder M. Compartmentalization of the Cell Cortex by Septins Is Required for Maintenance of Cell Polarity in Yeast. Molecular Cell 2000, 5: 841-851. PMID: 10882120, DOI: 10.1016/s1097-2765(00)80324-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsCarrier ProteinsCell CompartmentationCell Cycle ProteinsCell DivisionCell MembraneCell PolarityCytoplasmCytoskeletal ProteinsExocytosisFungal ProteinsMorphogenesisMyosin Heavy ChainsMyosin Type IIMyosin Type VProtein-Tyrosine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsConceptsCell polaritySpecialized plasma membrane domainsIsotropic bud growthPlasma membrane domainsBud neckMembrane domainsMother cellsCell cortexCell peripheryGrowth polaritySeptinsProper regulationBud surfaceBiological processesBud growthCell polarizationIsotropic growthCortical domainsExocytosisPatch stabilityActive siteCellsMyo2Sec5SPA2
1996
Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
Wirth J, Jensen K, Post P, Bement W, Mooseker M. Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail. Journal Of Cell Science 1996, 109: 653-661. PMID: 8907710, DOI: 10.1242/jcs.109.3.653.Peer-Reviewed Original ResearchConceptsProtein domainsHL-60 cellsRho/Rac familyNovel N-terminal domainGTPase-activating protein (GAP) domainUnconventional myosin heavy chainRas-like G proteinsPrimary structurePutative actin-binding siteAmino acidsFull-length primary structureSkeletal muscle myosin IIN-terminal domainAmino acid extensionActin-binding siteProtein kinase CNorthern blot analysisMuscle myosin IIRac familyDifferent human tissuesUndifferentiated HL-60 cellsRegulatory domainPutative zincRac GTPaseCell periphery