[HTML][HTML] ArgBP2, a multiple Src homology 3 domain-containing, Arg/Abl-interacting protein, is phosphorylated in v-Abl-transformed cells and localized in stress fibers …
B Wang, EA Golemis, GD Kruh - Journal of Biological Chemistry, 1997 - ASBMB
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 cells. ArgBP2 is widely expressed in …
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 cells. ArgBP2 is widely expressed in …