Shc has two distinct domains, amino-terminal and SH2 domain, which can interact with
activated growth factor receptors. Shc interacts with insulin receptor via Shc-amino-terminal …

Insulin stimulation of Chinese hamster ovary cells expressing the human insulin and
epidermal growth factor (EGF) receptors (CHO/IR/ER) resulted in the tyrosine …

Stimulation of the insulin receptor (IR) results in tyrosine phosphorylation of the intermediate
molecules insulin receptor substrate-1 (IRS-1), IRS-2, and Shc, which then couple the IR to …

Shc proteins contain a single SH2 domain, lack catalytic activity, and are substrates for
activated receptors for insulin, insulin-like growth factor-1 (IGF-1), and epidermal growth …

The SHC proteins have been implicated in insulin receptor (IR) signaling. In this study, we
used the sensitive two-hybrid assay of protein-protein interaction to demonstrate that SHC …

Shc is phosphorylated on Tyr-317, which serves as a docking site for Grb2. To investigate
the specific role of Shc phosphorylation and Shc· Grb2 coupling on insulin signaling, we …

The products of the shc gene appear to be substrates for activated oncogenic tyrosine
kinases, such as v-Src and v-Fps and activated tyrosine kinase receptors like the epidermal …

Insulin receptor substrate-1 (IRS-1) and Shc are two proteins implicated in intracellular
signal transduction. They are activated by an increasing number of extracellular signals …

Shc is phosphorylated on Tyr-239/240 and/or Tyr-317, which serves as a docking site for
Grb2. To clarify the relative involvement of Shc Tyr-239/240 and Tyr-317 in insulin-induced …

Multipin peptide synthesis has been employed to produce biotinylated 11-mer
phosphopeptides that account for every tyrosine residue in insulin receptor substrate-1 (IRS …