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FEBS Lett. 2007 Mar 6;581(5):853-7. Epub 2007 Feb 2.

Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl-terminal domain.

Author information

1
Unité de Pathogénie Microbienne Moléculaire, Inserm U786, Institut Pasteur, 75724 Paris Cedex 15, France.

Abstract

Shigella, the causative agent of bacillary dysentery, invades epithelial cells. Upon bacterial-cell contact, the type III bacterial effector IpaA binds to the cytoskeletal protein vinculin to promote actin reorganization required for efficient bacterial uptake. We show that the last 74 C-terminal residues of IpaA (A559) bind to human vinculin (HV) and promotes its association with actin filaments. Polymerisation experiments demonstrated that A559 was sufficient to induce HV-dependent partial capping of the barbed ends of actin filaments. These results suggest that IpaA regulates actin polymerisation/depolymerisation at sites of Shigella invasion by modulating the barbed end capping activity of vinculin.

PMID:
17289036
DOI:
10.1016/j.febslet.2007.01.057
[Indexed for MEDLINE]
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