beta-arrestin-1 competitively inhibits insulin-induced ubiquitination and degradation of insulin receptor substrate 1.

@article{Usui2004betaarrestin1CI,
  title={beta-arrestin-1 competitively inhibits insulin-induced ubiquitination and degradation of insulin receptor substrate 1.},
  author={Isao Usui and Takeshi Imamura and Jie Huang and Hiroaki Satoh and Sudha K Shenoy and Robert J Lefkowitz and Christopher J. Hupfeld and Jerrold M. Olefsky},
  journal={Molecular and cellular biology},
  year={2004},
  volume={24 20},
  pages={
          8929-37
        }
}
beta-arrestin-1 is an adaptor protein that mediates agonist-dependent internalization and desensitization of G-protein-coupled receptors (GPCRs) and also participates in the process of heterologous desensitization between receptor tyrosine kinases and GPCR signaling. In the present study, we determined whether beta-arrestin-1 is involved in insulin-induced insulin receptor substrate 1 (IRS-1) degradation. Overexpression of wild-type (WT) beta-arrestin-1 attenuated insulin-induced degradation of… CONTINUE READING
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