Drosophila ASPP Regulates C-Terminal Src Kinase Activity
| Autor: | Birgit L. Aerne, Nicolas Tapon, Paul F. Langton, Julien Colombani |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Ankyrins
Proline Blotting Western Regulator Biology General Biochemistry Genetics and Molecular Biology Animals Genetically Modified CSK Tyrosine-Protein Kinase src Homology Domains Drosophilidae Animals Drosophila Proteins Immunoprecipitation Phosphorylation Molecular Biology Cell growth Kinase Epithelial Cells Cell Biology Protein-Tyrosine Kinases Cell cycle biology.organism_classification Molecular biology Drosophila melanogaster Phenotype src-Family Kinases Signal Transduction Proto-oncogene tyrosine-protein kinase Src Developmental Biology |
| Zdroj: | Developmental Cell. 13(6):773-782 |
| ISSN: | 1534-5807 |
| DOI: | 10.1016/j.devcel.2007.11.005 |
| Popis: | Src-family kinases (SFKs) control a variety of biological processes, from cell proliferation and differentiation to cytoskeletal rearrangements. Abnormal activation of SFKs has been implicated in a wide variety of cancers and is associated with metastatic behavior (Yeatman, 2004). SFKs are maintained in an inactive state by inhibitory phosphorylation of their C-terminal region by C-terminal Src kinase (Csk). We have identified Drosophila Ankyrin-repeat, SH3-domain, and Proline-rich-region containing Protein (dASPP) as a regulator of Drosophila Csk (dCsk) activity. dASPP is the homolog of the mammalian ASPP proteins, which are known to bind to and stimulate the proapoptotic function of p53. We show that dASPP is a positive regulator of dCsk. First, dASPP loss-of-function strongly enhances the specific phenotypes of dCsk mutants in wing epithelial cells. Second, dASPP interacts physically with dCsk to potentiate the inhibitory phosphorylation of Drosophila Src (dSrc). Our results suggest a role for dASPP in maintaining epithelial integrity through dCsk regulation. |
| Databáze: | OpenAIRE |
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