Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake
| Autor: | M.S. Donnenberg, J.B. Kaper, B. Brett Finlay, Ilan Rosenshine |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Protein tyrosine phosphatase
SH2 domain Epithelium chemistry.chemical_compound Phosphorylation Tyrosine Internalization Cytoskeleton Protein Kinase C media_common General Neuroscience Protein-Tyrosine Kinases Genistein Neoplasm Proteins Cell biology Signal transduction Research Article Signal Transduction inorganic chemicals media_common.quotation_subject macromolecular substances Biology Models Biological General Biochemistry Genetics and Molecular Biology Alkaloids Escherichia coli Humans Enteropathogenic Escherichia coli Protein kinase A Molecular Biology Protein kinase C General Immunology and Microbiology Cell Membrane Genetic Complementation Test Tyrosine phosphorylation Cell Biology biochemical phenomena metabolism and nutrition Phosphoproteins Staurosporine Isoflavones Molecular biology Molecular Weight Kinetics enzymes and coenzymes (carbohydrates) chemistry Genes Bacterial bacteria HeLa Cells |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1992.tb05438.x |
| Popis: | Upon attachment to cultured HeLa cells, enteropathogenic Escherichia coli (EPEC) induces assembly of a complex cytoskeletal structure within the eucaryotic cell, localized beneath the adherent bacterium. In addition, EPEC induces its own internalization by non-phagocytic epithelial cells. We found that after binding to the epithelial cell surface, EPEC induces tyrosine phosphorylation of three eucaryotic proteins. The major phosphorylation substrate is a 90 kDa protein (Hp90). In correlation with Hp90 tyrosine phosphorylation, the EPEC-induced cytoskeletal structure also contained tyrosine phosphorylated proteins. Using tyrosine protein kinase inhibitors and EPEC mutants (cfm) that fail to induce Hp90 phosphorylation, we demonstrate that induction of Hp90 phosphorylation is involved in initiation of the cytoskeletal structure assembly and in bacterial uptake. Other non-invasive EPEC mutants (eae) are still able to induce Hp90 tyrosine phosphorylation and to initiate aggregation of the tyrosine phosphorylated proteins and some cytoskeleton components. However, eae mutants are deficient in nucleating the aggregates into an organized structure. |
| Databáze: | OpenAIRE |
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