ArgBP2, a Multiple Src Homology 3 Domain-containing, Arg/Abl-interacting Protein, Is Phosphorylated in v-Abl-transformed Cells and Localized in Stress Fibers and Cardiocyte Z-disks*

@article{Wang1997ArgBP2AM,
  title={ArgBP2, a Multiple Src Homology 3 Domain-containing, Arg/Abl-interacting Protein, Is Phosphorylated in v-Abl-transformed Cells and Localized in Stress Fibers and Cardiocyte Z-disks*},
  author={B. Wang and E. Golemis and G. Kruh},
  journal={The Journal of Biological Chemistry},
  year={1997},
  volume={272},
  pages={17542 - 17550}
}
  • B. Wang, E. Golemis, G. Kruh
  • Published 1997
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • Arg and c-Abl represent the mammalian members of the Abelson family of protein-tyrosine kinases. A novel Arg/Abl-binding protein, ArgBP2, was isolated using a segment of the Arg COOH-terminal domain as bait in the yeast two-hybrid system. ArgBP2 contains three COOH-terminal Src homology 3 domains, a serine/threonine-rich domain, and several potential Abl phosphorylation sites. ArgBP2 associates with and is a substrate of Arg and v-Abl, and is phosphorylated on tyrosine in v-Abl-transformed… CONTINUE READING
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