[HTML][HTML] A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells
ML Lupher, KA Reedquist, S Miyake… - Journal of biological …, 1996 - ASBMB
The protooncogene product Cbl has emerged as a novel signal transduction protein
downstream of a number of cell surface receptors coupled to tyrosine kinases. Recently, we
and others have reported the activation-dependent association of Cbl with the Syk and ZAP-
70 tyrosine kinases through presently undefined mechanisms. Potential Src homology 2 and
3 domain binding sites within the C-terminal half of Cbl mediate in vivo interactions with
several signaling proteins; however, the N-terminal transforming region (Cbl-N) lacks …
downstream of a number of cell surface receptors coupled to tyrosine kinases. Recently, we
and others have reported the activation-dependent association of Cbl with the Syk and ZAP-
70 tyrosine kinases through presently undefined mechanisms. Potential Src homology 2 and
3 domain binding sites within the C-terminal half of Cbl mediate in vivo interactions with
several signaling proteins; however, the N-terminal transforming region (Cbl-N) lacks …
