Drosophila Abelson interacting protein (dAbi) is a positive regulator of Abelson tyrosine kinase activity
Autor: | Hoffmann Fm, Juang Jl |
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Rok vydání: | 1999 |
Předmět: |
Cancer Research
Abelson murine leukemia virus Molecular Sequence Data Biology Transfection SH3 domain Evolution Molecular src Homology Domains Mice Species Specificity hemic and lymphatic diseases Consensus Sequence Genetics Animals Drosophila Proteins Humans Gene family Amino Acid Sequence Cloning Molecular Phosphorylation Kinase activity Oncogene Proteins v-abl Proto-Oncogene Proteins c-abl neoplasms Molecular Biology Adaptor Proteins Signal Transducing Homeodomain Proteins ABL Sequence Homology Amino Acid Kinase Binding protein Protein-Tyrosine Kinases Rats Cell biology Enzyme Activation Cytoskeletal Proteins Drosophila melanogaster Biochemistry Insect Proteins Carrier Proteins Protein Processing Post-Translational Sequence Alignment Tyrosine kinase Protein Binding |
Zdroj: | Oncogene. 18:5138-5147 |
ISSN: | 1476-5594 0950-9232 |
DOI: | 10.1038/sj.onc.1202911 |
Popis: | Human and mouse Abelson interacting proteins (Abi) are SH3-domain containing proteins that bind to the proline-rich motifs of the Abelson protein tyrosine kinase. We report a new member of this gene family, a Drosophila Abi (dAbi) that is a substrate for Abl kinase and that co-immunoprecipitates with Abl if the Abi SH3 domain is intact. We have identified a new function for both dAbi and human Abi-2 (hAbi-2). Both proteins activate the kinase activity of Abl as assayed by phosphorylation of the Drosophila Enabled (Ena) protein. Removal of the dAbi SH3 domain eliminates dAbi's activation of Abl kinase activity. dAbi is an unstable protein in cells and is present at low steady state levels but its protein level is increased coincident with phosphorylation by Abl kinase. Expression of the antisense strand of dAbi reduces dAbi protein levels and abolishes activation of Abl kinase activity. Modulation of Abi protein levels may be an important mechanism for regulating the level of Abl kinase activity in the cell. |
Databáze: | OpenAIRE |
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