Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics

Thierry Dubois; Olivia Paléotti; Alexander A. Mironov; Vincent Fraisier; Theresia E B Stradal; Maria Antonietta De Matteis; Michel Franco; Philippe Chavrier

doi:10.1038/ncb1244

Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics

Thierry Dubois, Olivia Paléotti, Alexander A. Mironov, Vincent Fraisier, Theresia E B Stradal, Maria Antonietta De Matteis, Michel Franco, Philippe Chavrier

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

Abstract

The small GTP-binding ADP-ribosylation factor 1 (ARF1) acts as a master regulator of Golgi structure and function through the recruitment and activation of various downstream effectors. It has been proposed that members of the Rho family of small GTPases also control Golgi function in coordination with ARF1, possibly through the regulation of Arp2/3 complex and actin polymerization on Golgi membranes. Here, we identify ARHGAP10 - a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1. We show that ARHGAP10 functions preferentially as a GAP for Cdc42 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity. Our results establish a role for ARHGAP10 in Golgi structure and function at the crossroads between ARF1 and Cdc42 signalling pathways.

Original language	English
Pages (from-to)	353-364
Number of pages	11
Journal	Nature Cell Biology
Volume	7
Issue number	4
DOIs	https://doi.org/10.1038/ncb1244
Publication status	Published - Apr 2005

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title = "Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics",

abstract = "The small GTP-binding ADP-ribosylation factor 1 (ARF1) acts as a master regulator of Golgi structure and function through the recruitment and activation of various downstream effectors. It has been proposed that members of the Rho family of small GTPases also control Golgi function in coordination with ARF1, possibly through the regulation of Arp2/3 complex and actin polymerization on Golgi membranes. Here, we identify ARHGAP10 - a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1. We show that ARHGAP10 functions preferentially as a GAP for Cdc42 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity. Our results establish a role for ARHGAP10 in Golgi structure and function at the crossroads between ARF1 and Cdc42 signalling pathways.",

author = "Thierry Dubois and Olivia Pal{\'e}otti and Mironov, {Alexander A.} and Vincent Fraisier and Stradal, {Theresia E B} and {De Matteis}, {Maria Antonietta} and Michel Franco and Philippe Chavrier",

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T1 - Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics

AU - Dubois, Thierry

AU - Paléotti, Olivia

AU - Mironov, Alexander A.

AU - Fraisier, Vincent

AU - Stradal, Theresia E B

AU - De Matteis, Maria Antonietta

AU - Franco, Michel

AU - Chavrier, Philippe

PY - 2005/4

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N2 - The small GTP-binding ADP-ribosylation factor 1 (ARF1) acts as a master regulator of Golgi structure and function through the recruitment and activation of various downstream effectors. It has been proposed that members of the Rho family of small GTPases also control Golgi function in coordination with ARF1, possibly through the regulation of Arp2/3 complex and actin polymerization on Golgi membranes. Here, we identify ARHGAP10 - a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1. We show that ARHGAP10 functions preferentially as a GAP for Cdc42 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity. Our results establish a role for ARHGAP10 in Golgi structure and function at the crossroads between ARF1 and Cdc42 signalling pathways.

AB - The small GTP-binding ADP-ribosylation factor 1 (ARF1) acts as a master regulator of Golgi structure and function through the recruitment and activation of various downstream effectors. It has been proposed that members of the Rho family of small GTPases also control Golgi function in coordination with ARF1, possibly through the regulation of Arp2/3 complex and actin polymerization on Golgi membranes. Here, we identify ARHGAP10 - a novel Rho GTPase-activating protein (Rho-GAP) that is recruited to Golgi membranes through binding to GTP-ARF1. We show that ARHGAP10 functions preferentially as a GAP for Cdc42 and regulates the Arp2/3 complex and F-actin dynamics at the Golgi through the control of Cdc42 activity. Our results establish a role for ARHGAP10 in Golgi structure and function at the crossroads between ARF1 and Cdc42 signalling pathways.

U2 - 10.1038/ncb1244

DO - 10.1038/ncb1244

M3 - Article

C2 - 15793564

SN - 1465-7392

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SP - 353

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JO - Nature Cell Biology

JF - Nature Cell Biology

IS - 4

ER -

Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics

Abstract

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