Phosphorylation of Enabled by the Drosophila Abelson Tyrosine Kinase Regulates the In Vivo Function and Protein-Protein Interactions of Enabled
| Autor: | Allen R. Comer, Shawn M. Ahern-Djamali, F. M. Hoffmann, Jyh-Lyh Juang, P. David Jackson |
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| Rok vydání: | 1998 |
| Předmět: |
ABL
Ena/Vasp homology proteins macromolecular substances Cell Biology Genes abl Biology Actin cytoskeleton Molecular biology DNA-Binding Proteins src Homology Domains hemic and lymphatic diseases Phosphoprotein Mutation Animals Phosphorylation Drosophila Tyrosine Signal transduction Cell Growth and Development Molecular Biology Tyrosine kinase Protein Binding Signal Transduction |
| Zdroj: | Molecular and Cellular Biology. 18:152-160 |
| ISSN: | 1098-5549 |
| Popis: | Drosophila Enabled (Ena) is a member of a family of cytoskeleton-associated proteins including mammalian vasodilator-stimulated phosphoprotein and murine Enabled that regulate actin cytoskeleton assembly. Mutations in Drosophila ena were discovered as dominant genetic suppressors of mutations in the Abelson tyrosine kinase (Abl), suggesting that Ena and Abl function in the same pathway or process. We have identified six tyrosine residues on Ena that are phosphorylated by Abl in vitro and in vivo. Mutation of these phosphorylation sites to phenylalanine partially impaired the ability of Ena to restore viability to ena mutant animals, indicating that phosphorylation is required for optimal Ena function. Phosphorylation of Ena by Abl inhibited the binding of Ena to SH3 domains in vitro, suggesting that one effect of Ena phosphorylation may be to modulate its association with other proteins. |
| Databáze: | OpenAIRE |
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