期刊
CELL HOST & MICROBE
卷 3, 期 1, 页码 39-47出版社
CELL PRESS
DOI: 10.1016/j.chom.2007.10.011
关键词
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资金
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI052354] Funding Source: NIH RePORTER
- NIAID NIH HHS [AI052354, R01 AI052354-03, R01 AI052354, R01 AI052354-02, R01 AI052354-04, R01 AI052354-05, R01 AI052354-01A1] Funding Source: Medline
Actin polymerization in the mammalian cytosol can be locally activated by mechanisms that relieve the autoinhibited state of N-WASP, an initiator of actin assembly, a process that also requires the protein Toca-1. Several pathogenic bacteria, including Shigella, exploit this host feature to infect and disseminate efficiently. The Shigella outer membrane protein IcsA recruits N-WASP, which upon activation at the bacterial surface mediates localized actin polymerization. The molecular role of Toca-1 in N-WASP activation during physiological or pathological actin assembly processes in intact mammalian cells remains unclear. We show that actin tail initiation by S. flexneri requires Toca-1 for the conversion of N-WASP from a closed inactive conformation to an open active one. While N-WASP recruitment is dependent on IcsA, Toca-1 recruitment is instead mediated by S. flexneri type III secretion effectors. Thus, S. flexneri independently hijacks two nodes of the N-WASP actin assembly pathway to initiate localized actin tail assembly.
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