Key result
Class IX myosin myr5 localizes to Shigella entry spots independently of GTPase or ATP binding.
Why the study?
Efficient control of Shigella-induced, rho-dependent cytoskeletal rearrangements is required to understand bacterial invasion of epithelial cells and the role of myr5 in this process.
The class IX myosin myr5 plays a functional role in the internalization of Shigella flexneri into epithelial cells.
May inform host-directed strategies against Shigella; leaves open whether myr5 is a viable therapeutic target.
Efficient control of Shigella-induced, rho-dependent cytoskeletal rearrangements seems to be required to shape the delicate cellular structures associated with bacterial invasion of epithelial cells. We therefore studied a class IX myosin and rho antagonist, the GTPase-activating protein (GAP) myr5, for a potential role in the bacterial entry process. We show that myr5 is recruited into bacterial entry spots. The recruitment pattern resembled that of rhoC or ezrin, but not rhoA, rac or CDC42, while in vitro GAP activity of myr5 was similar for rhoA, B or C. Analysis of myr5 mutants suggested that GTPase- or ATP-binding activites are not required for Shigella-induced recruitment of this atypical myosin to the bacterial entry site. Functional studies revealed a potential dual role of the myosin functions and the GAP module of myr5 for bacterial internalization.
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Graf et al. (2000) studied Shigella flexneri infection. myr5 (class IX myosin and rho antagonist) was evaluated on Role of myr5 in bacterial entry process. The class IX myosin myr5 is recruited to Shigella entry spots independently of GTPase- or ATP-binding activities, suggesting a dual role for its myosin functions and GAP module in internalization.
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