37-kDa Laminin Receptor Precursor Modulates Cytotoxic Necrotizing Factor 1–mediated RhoA Activation and Bacterial Uptake
| Autor: | Suk Jin Hong, Sooan Shin, Ted M. Dawson, Monique F. Stins, Kee Jun Kim, Daniel Goti, Valina L. Dawson, Kwang Sik Kim, Jin Woong Chung |
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| Rok vydání: | 2003 |
| Předmět: |
RHOA
Endothelium Bacterial Toxins Biology Biochemistry Cell Line Receptors Laminin Enzyme activator Escherichia coli medicine Protein Precursors Receptor Cytoskeleton Molecular Biology Escherichia coli Infections Cytotoxins cDNA library Escherichia coli Proteins Cell Biology Oligonucleotides Antisense Molecular biology Cell biology Enzyme Activation medicine.anatomical_structure Cell culture biology.protein lipids (amino acids peptides and proteins) Endothelium Vascular Signal transduction rhoA GTP-Binding Protein Protein Binding Signal Transduction |
| Zdroj: | Journal of Biological Chemistry. 278:16857-16862 |
| ISSN: | 0021-9258 |
| Popis: | Cytotoxic necrotizing factor 1 (CNF1) is a bacterial toxin known to activate Rho GTPases and induce host cell cytoskeleton rearrangements. The constitutive activation of Rho GTPases by CNF1 is shown to enhance bacterial uptake in epithelial cells and human brain microvascular endothelial cells. However, it is unknown how exogenous CNF1 exhibits such phenotypes in eukaryotic cells. Here, we identified 37-kDa laminin receptor precursor (LRP) as the receptor for CNF1 from screening the cDNA library of human brain microvascular endothelial cells by the yeast two-hybrid system using the N-terminal domain of CNF1 as bait. CNF1-mediated RhoA activation and bacterial uptake were inhibited by exogenous LRP or LRP antisense oligodeoxynucleotides, whereas they were increased in LRP-overexpressing cells. These findings indicate that the CNF1 interaction with LRP is the initial step required for CNF1-mediated RhoA activation and bacterial uptake in eukaryotic cells. |
| Databáze: | OpenAIRE |
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