English: Schematic representation of the intracellular regulation of proPC-PLC activity. Asymmetric polymerization of host actin at the bacterial surface results in actin-based motility, which facilitates direct bacterial cell-to-cell spread. During cell-to-cell spread, the bacterium becomes transiently trapped in a double membrane vacuole, which fuses with Lamp1-positive vesicles. ProPC-PLC secreted in the vacuole is activated by either a bacterial or a host protease subsequent to acidification of the vacuole. Upon lysis of the vacuole, which is mediated in part by the phospholipases, the bacterium gains access to the cytosol where secreted proPC-PLC is degraded by the proteasome.
Date
Source
Marquis et al 1997. Originally published in the Journal of Cell Biology. doi: 10.1083/jcb.137.6.1381.
Author
Hélène Marquis, Howard Goldfine, and Daniel A. Portnoy
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Under the following conditions:
attribution – You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
share alike – If you remix, transform, or build upon the material, you must distribute your contributions under the same or compatible license as the original.
{{Information |Description ={{en|1=Schematic representation of the intracellular regulation of proPC-PLC activity. Asymmetric polymerization of host actin at the bacterial surface results in actin-based motility, which facilitates direct bacterial cell