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  • Title: [Ubiquitination-mediated degradation of epidermal growth factor receptor].
    Author: Xiu X, Lü ZM.
    Journal: Zhongguo Yi Xue Ke Xue Yuan Xue Bao; 2005 Feb; 27(1):120-7. PubMed ID: 15782507.
    Abstract:
    After binding to its ligand, epidermal growth factor receptor (EGFR) dimerizes and is autophosphorylated. These events initiate the signal transduction process, which regulates a plethora of biologic activity. The duration and strength of these signals are controlled by many regulatory mechanisms, including downregulating activated EGFR primarily via endocytosis and ubiquitination-dependent lysomal degradation. The interaction between EGFR and the ubiquitin ligase Cbl/adaptor protein CIN85, as well as ESCRT complex recruitment play important roles in the process of downregulating EGFR. Tumorigenesis results when the de-sensitization process of EGFR is halted by its own mutation or a mutation that abrogates Cbl E3 ligase activity.
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