Search results for "MDia1"

showing 4 items of 4 documents

2013

Controlling the position of the nucleus is vital for a number of cellular processes from yeast to humans. In Drosophila nurse cells, nuclear positioning is crucial during dumping, when nurse cells contract and expel their contents into the oocyte. We provide evidence that in nurse cells, continuous filopodia-like actin cables, growing from the plasma membrane and extending to the nucleus, achieve nuclear positioning. These actin cables move nuclei away from ring canals. When nurse cells contract, actin cables associate laterally with the nuclei, in some cases inducing nuclear turning so that actin cables become partially wound around the nuclei. Our data suggest that a perinuclear actin mes…

0303 health sciencesbiologyArp2/3 complexActin remodelingmacromolecular substancesCell BiologyFilaminActin cytoskeletonGeneral Biochemistry Genetics and Molecular BiologyCell biology03 medical and health sciencesActin remodeling of neurons0302 clinical medicineProfilinbiology.proteinMDia1Molecular BiologyFilopodia030217 neurology & neurosurgery030304 developmental biologyDevelopmental BiologyDevelopmental Cell
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Small GTP-binding proteins of the Rho- and Ras-subfamilies are not involved in the actin rearrangements induced by attaching and effacingEscherichia …

1998

Attaching and effacing Escherichia coli (AEEC) are extracellular pathogens that induce the formation of actin-rich structures at their sites of attachment to eukaryotic host cells. We analysed whether small GTP-binding proteins of the Rho- and Ras-subfamilies, which control the cellular actin system, are essential for these bacterial-induced microfilament reorganizations. For this purpose we specifically inactivated them using the Clostridium difficile toxins TcdB-10463 and TcdB-1470. Such treatment led to a dramatic breakdown of the normal actin cytoskeleton, but did not abrogate the bacterial-induced actin rearrangements. Our data therefore indicate that the microfilament reorganizations …

Bacterial ToxinsExotoxinsArp2/3 complexmacromolecular substancesShiga ToxinsMicrofilamentMicrobiologyGTP-Binding ProteinsEscherichia coliGeneticsAnimalsHumansActin-binding proteinCytoskeletonMolecular BiologyActinbiologyClostridioides difficileActin remodelingActin cytoskeletonActinsActin CytoskeletonMicroscopy ElectronBiochemistryMicroscopy Electron Scanningras Proteinsbiology.proteinCattleMDia1HeLa CellsFEMS Microbiology Letters
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Rho protein-mediated changes in the structure of the actin cytoskeleton regulate human inducible NO synthase gene expression ☆ ☆This article contains…

2003

Rho proteins (Rho, Rac, Cdc 42) are known to control the organization of the actin cytoskeleton as well as gene expression. Inhibition of Rho proteins by Clostridium difficile toxin B disrupted the F-actin cytoskeleton and enhanced cytokine-induced inducible nitric oxide synthase (iNOS) expression in human epithelial cells. Also specific inhibition by Y-27632 of p160ROCK, which mediates Rho effects on actin fibers, caused a disruption of the actin cytoskeleton and a superinduction of cytokine-induced iNOS expression. Accordingly, direct disruption of the actin cytoskeleton by cytochalasin D, latrunculin B, or jasplakinolide enhanced cytokine-induced iNOS expression. The transcription factor…

Regulation of gene expressionActin remodelingClostridium difficile toxin Bmacromolecular substancesCell BiologyBiologyActin cytoskeletonMolecular biologyCell biologyProfilinSerum response factorbiology.proteinMDia1CytoskeletonExperimental Cell Research
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The actin-based motility of intracellularListeria monocytogenesis not controlled by small GTP-binding proteins of the Rho- and Ras-subfamilies

1999

In this study, we analyzed whether the actin-based motility of intracellular Listeria monocytogenes is controlled by the small GTP-binding proteins of the Rho- and Ras-subfamilies. These signalling proteins are key regulatory elements in the control of actin dynamics and their activity is essential for the maintenance of most cellular microfilament structures. We used the Clostridium difficile toxins TcdB-10463 and TcdB-1470 to specifically inactivate these GTP-binding proteins. Treatment of eukaryotic cells with either of these toxins led to a dramatic breakdown of the normal actin cytoskeleton, but did not abrogate the invasion of epithelial cells by L. monocytogenes and had no effect on …

Time FactorsArp2/3 complexClostridium difficile toxin Bmacromolecular substancesBiologyMicrofilamentMicrobiologyCell LineBacterial ProteinsGTP-Binding ProteinsGeneticsMolecular BiologyMicroscopy ConfocalMicroscopy VideoClostridioides difficileActin remodelingActin cytoskeletonListeria monocytogenesActinsCell biologyEndotoxinsProfilinParacytophagyMicroscopy Electron Scanningras Proteinsbiology.proteinMDia1FEMS Microbiology Letters
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