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• W1574278217 endingPage "494" @default.
• W1574278217 startingPage "483" @default.
• W1574278217 abstract "Cells permeabilized by the bacterial pore-forming toxin streptolysin O (SLO) reseal their plasma membrane in a Ca(2+) -dependent manner. Resealing involves Ca(2+) -dependent exocytosis of lysosomes, release of acid sphingomyelinase and rapid formation of endosomes that carry the transmembrane pores into the cell. The intracellular fate of the toxin-carrying endocytic vesicles, however, is still unknown. Here, we show that SLO pores removed from the plasma membrane by endocytosis are sorted into the lumen of lysosomes, where they are degraded. SLO-permeabilized cells contain elevated numbers of total endosomes, which increase gradually in size while transitioning from endosomes with flat clathrin coats to large multivesicular bodies (MVBs). Under conditions that allow endocytosis and plasma membrane repair, SLO is rapidly ubiquitinated and gradually degraded, in a process sensitive to inhibitors of lysosomal hydrolysis but not of proteasomes. The endosomes induced by SLO permeabilization become increasingly acidified and promote SLO degradation under normal conditions, but not in cells silenced for expression of Vps24, an ESCRT-III complex component required for the release of intraluminal vesicles into MVBs. Thus, cells dispose of SLO transmembrane pores by ubiquitination/ESCRT-dependent sorting into the lumen of late endosomes/lysosomes." @default.
• W1574278217 created "2016-06-24" @default.
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• W1574278217 date "2012-01-24" @default.
• W1574278217 modified "2023-10-14" @default.
• W1574278217 title "Toxin Pores Endocytosed During Plasma Membrane Repair Traffic into the Lumen of<scp>MVB</scp>s for Degradation" @default.
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• W1574278217 doi "https://doi.org/10.1111/j.1600-0854.2011.01323.x" @default.
• W1574278217 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3356596" @default.
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• W1574278217 hasPublicationYear "2012" @default.
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