Formin‐mediated actin polymerization promotes Salmonella invasion |
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| Authors: | Dorothy Truong Danielle Brabant Mikhail Bashkurov Leo C. K. Wan Virginie Braun Won Do Heo Tobias Meyer Laurence Pelletier John Copeland John H. Brumell |
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| Affiliation: | 1. Cell Biology Program, The Hospital for Sick Children, , Toronto, ON, Canada, M5G 1X8;2. Department of Molecular Genetics, University of Toronto, , Toronto, ON, Canada, M5S 1A8;3. Samuel Lunenfeld Research Institute, Mount Sinai Hospital, , Toronto, ON, Canada, M5G 1X5;4. Department of Biological Sciences and KI for the BioCentury, KAIST, , Daejeon, 305‐701 Korea;5. Chemical and Systems Biology, Stanford University Medical School, , Stanford, CA, 94305 USA;6. Department of Cellular and Molecular Medicine, University of Ottawa, , Ottawa, ON, Canada, K1H 8?M5;7. Institute of Medical Science, University of Toronto, , Toronto, ON, Canada, M5S 1A8;8. Sickkids IBD Centre, The Hospital for Sick Children, , Toronto, ON, Canada, M5G 1X8 |
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| Abstract: | Salmonella invade host cells using Type 3 secreted effectors, which modulate host cellular targets to promote actin rearrangements at the cell surface that drive bacterial uptake. The Arp2/3 complex contributes to Salmonella invasion but is not essential, indicating other actin regulatory factors are involved. Here, we show a novel role for FHOD1, a formin family member, in Salmonella invasion. FHOD1 and Arp2/3 occupy distinct microdomains at the invasion site and control distinct aspects of membrane protrusion formation. FHOD1 is phosphorylated during infection and this modification is required for promoting bacterial uptake by host cells. ROCK II, but not ROCK I, is recruited to the invasion site and is required for FHOD1 phosphorylation and for Salmonella invasion. Together, our studies revealan important phospho‐dependent FHOD1 actin polymerization pathway in Salmonella invasion. |
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