Abstract
The mechanisms leading to the ubiquitination and degradation of the activated c-Abl kinase have not yet been identified. We found that the multi-adaptor protein ArgBP2 links c-Abl to the ubiquitin ligase Cbl. Phosphorylation of Cbl and ArgBP2 by c-Abl resulted in the stabilization of their interactions, thus facilitating Cbl-induced ubiquitination and subsequent degradation of c-Abl and ArgBP2.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adaptor Proteins, Signal Transducing
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Animals
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CHO Cells
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Cricetinae
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Homeodomain Proteins / metabolism*
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Humans
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Hydrolysis
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Oncogene Protein v-cbl
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Phosphorylation
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Protein Binding
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Proto-Oncogene Proteins c-abl / metabolism*
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RNA-Binding Proteins
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Retroviridae Proteins, Oncogenic / metabolism*
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Two-Hybrid System Techniques
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Ubiquitin / metabolism*
Substances
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Adaptor Proteins, Signal Transducing
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Homeodomain Proteins
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Oncogene Protein v-cbl
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RNA-Binding Proteins
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Retroviridae Proteins, Oncogenic
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SORBS2 protein, human
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Ubiquitin
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Proto-Oncogene Proteins c-abl