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={Bingbing Wang and Erica A Golemis and Gary D. Kruh},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 28},
  pages={17542-50}
}
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

Citations

Publications citing this paper.
Showing 1-10 of 40 extracted citations

Impaired Dendritic Development and Memory in Sorbs2 Knock-Out Mice.

The Journal of neuroscience : the official journal of the Society for Neuroscience • 2016
View 7 Excerpts
Highly Influenced

Palladin , a novel microfilament protein

View 3 Excerpts
Highly Influenced

Fishing out proteins that bind to titin

The Journal of cell biology • 2001
View 2 Excerpts
Highly Influenced

Comparative proteomics analysis of myocardium in mouse model of diabetic cardiomyopathy using the iTRAQ technique.

Advances in clinical and experimental medicine : official organ Wroclaw Medical University • 2018

Similar Papers

Loading similar papers…