Ubiquitination-mediated degradation of epidermal growth factor receptor.
- Author:
Xia XIU
1
;
Zhi-min LÜ
Author Information
1. Department of Radiotherapy, Beijing Hospital, Beijing 100730, China.
- Publication Type:Journal Article
- MeSH:
Adaptor Proteins, Signal Transducing;
metabolism;
Animals;
Down-Regulation;
Endocytosis;
Epidermal Growth Factor;
pharmacology;
Humans;
Mutation;
Proto-Oncogene Proteins c-cbl;
metabolism;
Receptor, Epidermal Growth Factor;
genetics;
metabolism;
Signal Transduction;
Ubiquitin;
metabolism
- From:
Acta Academiae Medicinae Sinicae
2005;27(1):120-127
- CountryChina
- Language:Chinese
-
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.
