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- W2099284920 abstract "ABSTRACT ExoU is a potent phospholipase A 2 effector protein secreted by the type III secretion system of Pseudomonas aeruginosa . By cleaving plasma membrane phospholipids, it causes rapid lysis of eukaryotic cells. However, ExoU does not exhibit activity on its own but instead requires eukaryotic cell cofactors for activation. Ubiquitin and ubiquitinated proteins have been shown to activate ExoU, but previous work suggested that other cofactors are also involved. In this study, we demonstrate that phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] is another important coactivator of ExoU. PI(4,5)P2 works synergistically with ubiquitin to greatly enhance the phospholipase A 2 activity of ExoU. Distinct residues of ExoU were critical for activation by PI(4,5)P2 and by ubiquitin, indicating that these factors activate ExoU by discrete mechanisms. In support of the biological relevance of PI(4,5)P2 coactivation, a yeast mutant with reduced PI(4,5)P2 levels was less susceptible to the cytotoxic activity of ExoU. Together, these findings further elaborate the molecular mechanism of ExoU." @default.
- W2099284920 created "2016-06-24" @default.
- W2099284920 creator A5001810058 @default.
- W2099284920 creator A5036755430 @default.
- W2099284920 date "2013-08-01" @default.
- W2099284920 modified "2023-09-23" @default.
- W2099284920 title "Phosphatidylinositol 4,5-Bisphosphate Is a Novel Coactivator of the Pseudomonas aeruginosa Cytotoxin ExoU" @default.
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- W2099284920 doi "https://doi.org/10.1128/iai.00414-13" @default.
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