Sökning: id:"swepub:oai:DiVA.org:liu-99622" >
Deamidation of Cdc4...
Deamidation of Cdc42 and Rac by Escherichia coli cytotoxic necrotizing factor 1 : activation of c-Jun N-terminal kinase in HeLa cells
-
- Lerm, Maria (författare)
- Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany
-
- Selzer, J. (författare)
- Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany
-
- Hoffmeyer, A. (författare)
- Institut für medizinische Strahlenkunde und Zellforschung, Universität Würzburg, Germany
-
visa fler...
-
- Rapp, U. R. (författare)
- Institut für medizinische Strahlenkunde und Zellforschung, Universität Würzburg, Germany
-
- Aktories, K. (författare)
- Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany
-
- Schmidt, G. (författare)
- Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany
-
visa färre...
-
(creator_code:org_t)
- American Society for Microbiology, 1999
- 1999
- Engelska.
-
Ingår i: Infection and Immunity. - : American Society for Microbiology. - 0019-9567 .- 1098-5522. ; 67:2, s. 496-503
- Relaterad länk:
-
http://iai.asm.org/c...
-
visa fler...
-
https://urn.kb.se/re...
-
visa färre...
Abstract
Ämnesord
Stäng
- Recently, Escherichia coli cytotoxic necrotizing factor 1 (CNF1) was shown to activate the low-molecular-mass GTPase RhoA by deamidation of Gln63, thereby inhibiting intrinsic and GTPase-activating protein (GAP)-stimulated GTPase activities (G. Schmidt, P. Sehr, M. Wilm, J. Selzer, M. Mann, and K. Aktories, Nature 387:725-729, 1997; G. Flatau, E. Lemichez, M. Gauthier, P. Chardin, S. Paris, C. Fiorentini, and P. Boquet, Nature 387:729-733, 1997). Here we report that in addition to RhoA, Cdc42 and Rac also are targets for CNF1 in vitro and in intact cells. Treatment of HeLa cells with CNF1 induced a transient formation of microspikes and formation of membrane ruffles. CNF1 caused a transient 10- to 50-fold increase in the activity of the c-Jun N-terminal kinase. Tryptic peptides of Cdc42 obtained from CNF1-treated cells by immunoprecipitation exhibited an increase in mass of 1 Da compared to control peptides, indicating the deamidation of glutamine 61 by the toxin. The same increase in mass was observed with the respective peptides obtained from CNF1-modified recombinant Cdc42 and Rac1. Modification of recombinant Cdc42 and Rac1 by CNF1 inhibited intrinsic and GAP-stimulated GTPase activities and retarded binding of 2'(3')-O-(N-methylanthraniloyl)GDP. The data suggest that recombinant as well as cellular Cdc42 and Rac are substrates for CNF1.
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas