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MBC in Press, published online ahead of print March 15, 2006
Mol. Biol. Cell 10.1091/mbc.E05-09-0876

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Submitted on September 20, 2005
Revised on February 24, 2006
Accepted on March 6, 2006

CNF1-induced Ubiquitylation and Proteasome Destruction of Activated RhoA Is Impaired in Smurf1-/- Cells

Laurent Boyer,* Laurent Turchi,{dagger} Benoit Desnues,{ddagger} Anne Doye,* Gilles Ponzio,{dagger} Jean-louis Mege,{ddagger} Motozo Yamashita,{sect} Ying E. Zhang,{sect} Jacques Bertoglio,|| Gilles Flatau,* Patrice Boquet,* and Emmanuel Lemichez*

*Faculté de Médecine, INSERM, U627, 06107 Nice Cedex 2, France; {dagger}Faculté de Médecine, INSERM, U634, 06107 Nice Cedex 2, France; {ddagger}Université de la Méditerranée, Unité des Rickettsies, CNRS, UMR, 6020, Faculté de Médecine, 13385 Marseille, France; {sect}Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892; ||Faculté de Pharmacie, INSERM, U461, Paris-XI, 92290 Chatenay-Malabry, France

Monitoring Editor: Ralph Isberg

Ubiquitylation of RhoA has emerged as an important aspect of both the virulence of Escherichia coli producing CNF1-toxin and the establishment of the polarity of eukaryotic cells. Owing to the molecular activity of CNF1, we have investigated the relationship between permanent activation of RhoA catalyzed by CNF1 and subsequent ubiquitylation of RhoA by Smurf1. Using Smurf1-deficient cells and by RNAi-mediated Smurf1 knock-down we demonstrate that Smurf1 is a rate-limiting and specific factor of the ubiquitin-mediated proteasomal degradation of activated-RhoA. We further show that the cancer cell lines HEp-2, HEK293 and Vero are specifically deficient in ubiquitylation of either activated-Rac, Cdc42 or Rho, respectively. In contrast, CNF1 produced the cellular depletion of all three isoforms of Rho proteins in the primary human cell types we have tested. We demonstrate that ectopic expression of Smurf1 in Vero cells, deficient for RhoA ubiquitylation, restores ubiquitylation of the activated forms of RhoA. We conclude here that Smurf1 ubiquitylates activated-RhoA and that, in contrast to human primary cell types, some cancer cell lines have a lower ubiquitylation capacity of specific Rho proteins. Thus, both CNF1 and TGF-beta trigger activated-RhoA ubiquitylation through Smurf1 ubiquitin-ligase.

Address correspondence to: Emmanuel Lemichez (lemichez{at}unice.fr)




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