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.
Artigo
em Chinês
| 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.
Texto completo:
DisponíveL
Índice:
WPRIM (Pacífico Ocidental)
Assunto principal:
Farmacologia
/
Transdução de Sinais
/
Regulação para Baixo
/
Ubiquitina
/
Proteínas Adaptadoras de Transdução de Sinal
/
Endocitose
/
Fator de Crescimento Epidérmico
/
Proteínas Proto-Oncogênicas c-cbl
/
Receptores ErbB
/
Genética
Limite:
Animais
/
Humanos
Idioma:
Chinês
Revista:
Acta Academiae Medicinae Sinicae
Ano de publicação:
2005
Tipo de documento:
Artigo
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