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© Research
Publication : FEBS letters

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

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in FEBS letters - 02 Feb 2007

Ramarao N, Le Clainche C, Izard T, Bourdet-Sicard R, Ageron E, Sansonetti PJ, Carlier MF, Tran Van Nhieu G

Link to Pubmed [PMID] – 17289036

FEBS Lett. 2007 Mar;581(5):853-7

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.