Ubiquitination-mediated degradation of epidermal growth factor receptor / 中国医学科学院学报
Acta Academiae Medicinae Sinicae
;
(6): 120-127, 2005.
Article
in Chinese
| WPRIM
| ID: wpr-343754
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pharmacology
/
Signal Transduction
/
Down-Regulation
/
Ubiquitin
/
Adaptor Proteins, Signal Transducing
/
Endocytosis
/
Epidermal Growth Factor
/
Proto-Oncogene Proteins c-cbl
/
ErbB Receptors
/
Genetics
Limits:
Animals
/
Humans
Language:
Chinese
Journal:
Acta Academiae Medicinae Sinicae
Year:
2005
Type:
Article
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