Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors.
The anthrax toxin is a tripartite toxin, where the two enzymatic subunits require the third subunit, the protective antigen (PA), to interact with cells and be escorted to their cytoplasmic targets. PA binds to cells via one of two receptors, TEM8 and CMG2. Interestingly, the toxin times and trigger...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2010-03-01
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| Series: | PLoS Pathogens |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20221438/pdf/?tool=EBI |
| _version_ | 1811173564515090432 |
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| author | Laurence Abrami Mirko Bischofberger Béatrice Kunz Romain Groux F Gisou van der Goot |
| author_facet | Laurence Abrami Mirko Bischofberger Béatrice Kunz Romain Groux F Gisou van der Goot |
| author_sort | Laurence Abrami |
| collection | DOAJ |
| description | The anthrax toxin is a tripartite toxin, where the two enzymatic subunits require the third subunit, the protective antigen (PA), to interact with cells and be escorted to their cytoplasmic targets. PA binds to cells via one of two receptors, TEM8 and CMG2. Interestingly, the toxin times and triggers its own endocytosis, in particular through the heptamerization of PA. Here we show that PA triggers the ubiquitination of its receptors in a beta-arrestin-dependent manner and that this step is required for clathrin-mediated endocytosis. In addition, we find that endocytosis is dependent on the heterotetrameric adaptor AP-1 but not the more conventional AP-2. Finally, we show that endocytosis of PA is strongly dependent on actin. Unexpectedly, actin was also found to be essential for efficient heptamerization of PA, but only when bound to one of its 2 receptors, TEM8, due to the active organization of TEM8 into actin-dependent domains. Endocytic pathways are highly modular systems. Here we identify some of the key players that allow efficient heptamerization of PA and subsequent ubiquitin-dependent, clathrin-mediated endocytosis of the anthrax toxin. |
| first_indexed | 2024-04-10T17:49:02Z |
| format | Article |
| id | doaj.art-c078b9bbbd4c420b8e7134fb30dc94ab |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-04-10T17:49:02Z |
| publishDate | 2010-03-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-c078b9bbbd4c420b8e7134fb30dc94ab2023-02-02T22:56:51ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742010-03-0163e100079210.1371/journal.ppat.1000792Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors.Laurence AbramiMirko BischofbergerBéatrice KunzRomain GrouxF Gisou van der GootThe anthrax toxin is a tripartite toxin, where the two enzymatic subunits require the third subunit, the protective antigen (PA), to interact with cells and be escorted to their cytoplasmic targets. PA binds to cells via one of two receptors, TEM8 and CMG2. Interestingly, the toxin times and triggers its own endocytosis, in particular through the heptamerization of PA. Here we show that PA triggers the ubiquitination of its receptors in a beta-arrestin-dependent manner and that this step is required for clathrin-mediated endocytosis. In addition, we find that endocytosis is dependent on the heterotetrameric adaptor AP-1 but not the more conventional AP-2. Finally, we show that endocytosis of PA is strongly dependent on actin. Unexpectedly, actin was also found to be essential for efficient heptamerization of PA, but only when bound to one of its 2 receptors, TEM8, due to the active organization of TEM8 into actin-dependent domains. Endocytic pathways are highly modular systems. Here we identify some of the key players that allow efficient heptamerization of PA and subsequent ubiquitin-dependent, clathrin-mediated endocytosis of the anthrax toxin.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20221438/pdf/?tool=EBI |
| spellingShingle | Laurence Abrami Mirko Bischofberger Béatrice Kunz Romain Groux F Gisou van der Goot Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. PLoS Pathogens |
| title | Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. |
| title_full | Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. |
| title_fullStr | Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. |
| title_full_unstemmed | Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. |
| title_short | Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. |
| title_sort | endocytosis of the anthrax toxin is mediated by clathrin actin and unconventional adaptors |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20221438/pdf/?tool=EBI |
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