Abl kinase interacts with and phosphorylates vinexin
| Autor: | Tomoyuki Shishido, Masaru Mitsushima, Kazumitsu Ueda, Honami Takahashi, Noriyuki Kioka |
|---|---|
| Rok vydání: | 2006 |
| Předmět: |
Membrane ruffles
Biophysics macromolecular substances Biology Biochemistry SH3 domain c-Abl src Homology Domains Mice Membrane Microdomains Structural Biology hemic and lymphatic diseases Chlorocebus aethiops Genetics Animals Point Mutation Tyrosine Phosphorylation Proto-Oncogene Proteins c-abl Molecular Biology neoplasms Cytoskeleton Adaptor Proteins Signal Transducing Focal Adhesions ABL Actin cytoskeleton Signal transducing adaptor protein Cell Biology Molecular biology Actins Cell biology Rats SH3 Astrocytes COS Cells NIH 3T3 Cells Signal transduction Tyrosine kinase Protein Processing Post-Translational Vinexin Protein Binding Signal Transduction |
| Zdroj: | FEBS letters. 580(17) |
| ISSN: | 0014-5793 |
| Popis: | Non-receptor tyrosine kinase Abl is a well known regulator of the actin-cytoskeleton, including the formation of stress fibers and membrane ruffles. Vinexin is an adapter protein consisting of three SH3 domains, and involved in signal transduction and the reorganization of actin cytoskeleton. In this study, we found that vinexin alpha as well as beta interacts with c-Abl mainly through the third SH3 domain, and that vinexin and c-Abl were colocalized at membrane ruffles in rat astrocytes. This interaction was reduced by latrunculin B, suggesting an F-actin-mediated regulatory mechanism. We also found that vinexin alpha but not beta was phosphorylated at tyrosine residue when c-Abl or v-Abl was co-expressed. A mutational analysis identified tyrosine 127 on vinexin alpha as a major site of phosphorylation by c- or v-Abl. These results suggest that vinexin alpha is a novel substrate for Abl. |
| Databáze: | OpenAIRE |
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