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

Nalini Ramarao; Christophe Le Clainche; Tina Izard; Raphaëlle Bourdet-Sicard; Elisabeth Ageron; Philippe J. Sansonetti; Marie France Carlier; Guy Tran Van Nhieu

doi:10.1016/j.febslet.2007.01.057

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

Nalini Ramarao, Christophe Le Clainche, Tina Izard, Raphaëlle Bourdet-Sicard, Elisabeth Ageron, Philippe J. Sansonetti, Marie France Carlier, Guy Tran Van Nhieu

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	853-857
Number of pages	5
Journal	FEBS Letters
Volume	581
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2007.01.057
Publication status	Published - 6 Mar 2007
Externally published	Yes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Actin
Capping
IpaA
Shigella
Vinculin

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10.1016/j.febslet.2007.01.057

Cite this

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title = "Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl-terminal domain",

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.",

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author = "Nalini Ramarao and \{Le Clainche\}, Christophe and Tina Izard and Rapha{\"e}lle Bourdet-Sicard and Elisabeth Ageron and Sansonetti, \{Philippe J.\} and Carlier, \{Marie France\} and \{Tran Van Nhieu\}, Guy",

year = "2007",

month = mar,

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doi = "10.1016/j.febslet.2007.01.057",

language = "English",

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pages = "853--857",

journal = "FEBS Letters",

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TY - JOUR

T1 - Capping of actin filaments by vinculin activated by the Shigella IpaA carboxyl-terminal domain

AU - Ramarao, Nalini

AU - Le Clainche, Christophe

AU - Izard, Tina

AU - Bourdet-Sicard, Raphaëlle

AU - Ageron, Elisabeth

AU - Sansonetti, Philippe J.

AU - Carlier, Marie France

AU - Tran Van Nhieu, Guy

PY - 2007/3/6

Y1 - 2007/3/6

N2 - 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.

AB - 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.

KW - Actin

KW - Capping

KW - IpaA

KW - Shigella

KW - Vinculin

U2 - 10.1016/j.febslet.2007.01.057

DO - 10.1016/j.febslet.2007.01.057

M3 - Article

C2 - 17289036

AN - SCOPUS:33847115716

SN - 0014-5793

VL - 581

SP - 853

EP - 857

JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

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

Abstract

UN SDGs

Keywords

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