Journal
EXPERIMENTAL CELL RESEARCH
Volume 315, Issue 12, Pages 2001-2011Publisher
ELSEVIER INC
DOI: 10.1016/j.yexcr.2009.04.003
Keywords
Bacterial infection; Attaching and effacing; Actin; Cytoskeleton; Synapse
Categories
Funding
- National Institutes of Health [AI062773, AI46454, DK060049, DK043351]
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The common gastrointestinal pathogens enteropathogenic Escherichia coli (EPEC) and Salmonella typhimurium both reorganize the gut epithelial cell actin cytoskeleton to mediate pathogenesis, utilizing mimicry of the host signaling apparatus. The PDZ domain-containing protein Shank3, is a large cytoskeletal scaffold protein with known functions in neuronal morphology and synaptic signaling, and is also capable of acting as a scaffolding adaptor during Ret tyrosine kinase signaling in epithelial cells. Using immunofluorescent and functional RNA-interference approaches we show that Shank3 is present in both EPEC- and S. typhimurium-induced actin rearrangements and is required for optimal EPEC pedestal formation. We propose that Shank3 is one of a number of host synaptic proteins likely to play key roles in bacteria-host interactions. (C) 2009 Elsevier Inc. All rights reserved.
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