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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6634
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pubmed:dateCreated |
1997-7-9
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pubmed:abstractText |
The actin cytoskeleton is regulated by GTP-hydrolysing proteins, the Rho GTPases, which act as molecular switches in diverse signal-transduction processes. Various bacterial toxins can inactivate Rho GTPases by ADP-ribosylation or glucosylation. Previous research has identified Rho proteins as putative targets for Escherichia coli cytotoxic necrotizing factors 1 and 2 (CNF1 and 2). These toxins induce actin assembly and multinucleation in culture cells. Here we show that treatment of RhoA with CNF1 inhibits the intrinsic GTPase activity of RhoA and completely blocks GTPase activity stimulated by the Rho-GTPase-activating protein (rhoGAP). Analysis by mass spectrometry and amino-acid sequencing of proteolytic peptides derived from CNF1-treated RhoA indicate that CNF1 induces deamidation of a glutamine residue at position 63 (Gln 63) to give constitutively active Rho protein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2'(3')-O-(N-methyl)anthraniloylguano...,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose,
http://linkedlifedata.com/resource/pubmed/chemical/Anthranilic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cytotoxic necrotizing factor type 1,
http://linkedlifedata.com/resource/pubmed/chemical/rho GTPase-activating protein,
http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
387
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
725-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9192900-3T3 Cells,
pubmed-meshheading:9192900-Actins,
pubmed-meshheading:9192900-Adenosine Diphosphate Ribose,
pubmed-meshheading:9192900-Amino Acid Sequence,
pubmed-meshheading:9192900-Animals,
pubmed-meshheading:9192900-Anthranilic Acids,
pubmed-meshheading:9192900-Bacterial Toxins,
pubmed-meshheading:9192900-Cytoskeleton,
pubmed-meshheading:9192900-Cytotoxins,
pubmed-meshheading:9192900-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:9192900-Escherichia coli,
pubmed-meshheading:9192900-Escherichia coli Proteins,
pubmed-meshheading:9192900-GTP Phosphohydrolases,
pubmed-meshheading:9192900-GTP-Binding Proteins,
pubmed-meshheading:9192900-GTPase-Activating Proteins,
pubmed-meshheading:9192900-Glutamine,
pubmed-meshheading:9192900-Glycosylation,
pubmed-meshheading:9192900-Guanosine Triphosphate,
pubmed-meshheading:9192900-Mass Spectrometry,
pubmed-meshheading:9192900-Mice,
pubmed-meshheading:9192900-Microinjections,
pubmed-meshheading:9192900-Molecular Sequence Data,
pubmed-meshheading:9192900-Molecular Weight,
pubmed-meshheading:9192900-Recombinant Fusion Proteins,
pubmed-meshheading:9192900-rhoA GTP-Binding Protein
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pubmed:year |
1997
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pubmed:articleTitle |
Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1.
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pubmed:affiliation |
Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany.
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pubmed:publicationType |
Journal Article
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