Search results for "Polarisome"

showing 2 items of 2 documents

Fertility and Polarized Cell Growth Depends on eIF5A for Translation of Polyproline-Rich Formins in Saccharomyces cerevisiae

2014

eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during …

TranslationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalForminsRNA-binding proteinSaccharomyces cerevisiaeInvestigationsPeptide Initiation FactorsMorphogenesisGeneticsQc-SNARE ProteinsPolyproline helixPolarisomeGeneticsMatingbiologyMicrofilament ProteinsMembrane ProteinsRNA-Binding ProteinsTranslation (biology)Polarized growthbiology.organism_classificationActinsProtein Structure TertiaryCell biologyCytoskeletal ProteinsMating of yeastForminsMutationbiology.proteinEIF5APeptidesRibosomesEIF5A
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Rot1 plays an antagonistic role to Clb2 in actin cytoskeleton dynamics throughout the cell cycle.

2007

ROT1 is an essential gene whose inactivation causes defects in cell cycle progression and morphogenesis in budding yeast. Rot1 affects the actin cytoskeleton during the cell cycle at two levels. First, it is required for the maintenance of apical growth during bud growth. Second, Rot1 is necessary to polarize actin cytoskeleton to the neck region at the end of mitosis; because of this defect, rot1 cells do not properly form a septum to complete cell division. The inability to polarize the actin cytoskeleton at the end of mitosis is not due to a defect in the recruitment of the polarisome scaffold protein Spa2 or the actin cytoskeleton regulators Cdc42 and Cdc24 in the neck region. Previous …

Saccharomyces cerevisiae ProteinsGenes FungalArp2/3 complexmacromolecular substancesSaccharomyces cerevisiaeCyclin BActin remodeling of neuronsGene Expression Regulation FungalCDC2-CDC28 KinasesCytoskeletonCytoskeletonPolarisomebiologyCell CycleActin remodelingCell PolarityMembrane ProteinsCell BiologyActin cytoskeletonActinsCell biologyProfilinParacytophagyMutationbiology.proteinMolecular ChaperonesJournal of cell science
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