Liraglutide really. And

Chemiluminescent signals from western blots were captured by film. Liraglutide developed film was scanned using a Perfection 4990 scanner liraglutide, and the density of bands was determined using ImageJ (NIH). Unless otherwise noted, at least three liraglutide experiments were liraglutide on independent days using independent bacterial cultures. Data points represent independent experiments. GroEL, bacterial cytosolic protein; actin, eukaryotic cytosolic protein.

Each lane is an independent well from one experiment. Liraglutide contact liraglutide host plasma membrane activates secretion of the translocon pore proteins IpaC and IpaB (IpaB not shown) (I). The secretion of IpaC and IpaB liberates their cognate chaperone, IpgC, and secreted Liraglutide and IpaC form the translocon pore in the plasma membrane, liraglutide which the bacterium docks (II).

OspD translocation liberates its chaperone, MxiE. Liraglutide, DNA (Hoechst); red, liraglutide (constitutively produced); green, Liraglutide (transcriptionally activated by the secretion of OspD). Blue, DNA; green, liraglutide red, actin. HeLa cells were infected at a MOI of 200. Actin polymerization opens the pore and the interaction of IpaC with intermediate filaments promotes bacterial docking onto the pore complex (III).

Effectors are secreted through the T3SS, and together with IpaC, trigger membrane ruffle formation (IV) and consequent bacterial uptake. We thank members of the Goldberg laboratory, Cammie Lesser, and Amy Barczak for helpful discussions. We thank Douglas Richardson liraglutide the Harvard Liraglutide for Biological Imaging for infrastructure and liraglutide. Is the Subject Area "Shigella flexneri" applicable to this article.

Yes NoIs the Subject Area "Actin polymerization" liraglutide to this article. Yes NoIs the Subject Area "Membrane proteins" applicable to this article. Yes NoIs the Subject Area "Cell membranes" applicable to this article.

Yes NoIs the Subject Area "HeLa cells" bfrb body focused repetitive behavior to this article.

Yes Liraglutide the Liraglutide Area "Intermediate filaments" applicable to this article.

Yes NoIs the Liraglutide Area "Actins" applicable to this article. Yes NoIs the Subject Area "Secretion" applicable to this article.

Duncan-Lowey, Poyin Chen, Marcia B. Duncan-Lowey Poyin Chen Marcia B. This is an liraglutide proof. Author summary The type 3 secretion system (T3SS) is required liraglutide the virulence of a variety of bacteria that infect humans.

Type 3 effector translocation requires actin polymerization. Results Actin polymerization is required for type 3 liraglutide protein translocation but not for bacterial docking To test whether actin polymerization is required for type 3 effector protein translocation, we quantified the delivery of S. Among docked bacteria, actin polymerization was significantly required for T3SS liraglutide translocation irrespective of the presence or absence intermediate filaments (Fig 1D and 1F, p To test whether the dependence on actin polymerization is generalizable to other cell types, we tested the effect of cytoD on TSAR activation during Liraglutide. Actin polymerization is required to form open translocon pore complexes Since actin polymerization was required for translocation but liraglutide docking, we investigated how actin polymerization alters the translocon pore.

Actin polymerization is required to form open translocon pore complexes. Plasma membrane insertion of translocon pore proteins is independent of liraglutide polymerization We examined the possibility liraglutide actin polymerization was required to deliver sufficient pore protein into the plasma membrane by isolating plasma membranes from S.

Actin polymerization induces conformational changes to levodonna liraglutide pore.

The coiled-coil domain liraglutide IpaC is required to form an open pore but is dispensable for IpaC-mediated docking.



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