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Proteasomal degradation of cytotoxic necrotizing factor 1-activated rac
Albert-Ludwigs-Universität Freiburg, Germany.
Albert-Ludwigs-Universität Freiburg, Germany.
Institut für Toxikologie, Mainz, Germany.
Albert-Ludwigs-Universität Freiburg, Germany.
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2002 (English)In: Infection and Immunity, ISSN 0019-9567, E-ISSN 1098-5522, Vol. 70, no 8, 4053-4058 p.Article in journal (Refereed) Published
Abstract [en]

The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli has been shown to activate members of the Rho family by deamidation of glutamine 63. This amino acid is essential for hydrolysis of GTP, and any substitution results in a constitutively active Rho. Activation of Rho induces the formation of stress fibers, filopodia, and membrane ruffles due to activation of RhoA, Cdc42, and Rac, respectively. Here we show that the level of endogenous Rac decreased in CNF1-treated HEK293 and HeLa cells. The amount of mRNA remained unaffected, leaving the possibility that Rac is subject to proteolytic degradation. Treatment of cells with lactacystin, an inhibitor of the 26S proteasome, protected Rac from degradation. We have previously shown that CNF1 activates the c-Jun N-terminal kinase (JNK) only transiently in HeLa cells (M. Lerm, J. Selzer, A. Hoffmeyer, U. R. Rapp, K. Aktories, and G. Schmidt, Infect. Immun. 67:496-503, 1998). Here we show that CNF1-induced JNK activation is stabilized in the presence of lactacystin. The data indicate that Rac is degraded by a proteasome-dependent pathway in CNF1-treated cells.

Place, publisher, year, edition, pages
American Society for Microbiology , 2002. Vol. 70, no 8, 4053-4058 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-99623DOI: 10.1128/IAI.70.8.4053-4058.2002PubMedID: 12117911OAI: diva2:657398
Available from: 2013-10-18 Created: 2013-10-18 Last updated: 2013-10-28Bibliographically approved

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Lerm, Maria
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