EPH受体A2
自磷酸化
配体(生物化学)
癌症研究
信号转导衔接蛋白
受体酪氨酸激酶
磷酸化
细胞生物学
受体
酪氨酸激酶
信号转导
刺激
生物
化学
生物化学
蛋白激酶A
内分泌学
作者
Jennifer Walker‐Daniels,David J. Riese,Michael S. Kinch
出处
期刊:PubMed
日期:2002-11-01
卷期号:1 (1): 79-87
被引量:67
摘要
The EphA2 receptor protein tyrosine kinase is overexpressed and functionally altered in a large number of human carcinomas. Despite its elevated levels in cancer, the EphA2 on the surface of malignant cells demonstrates lower levels of ligand binding and tyrosine phosphorylation than the EphA2 on non-transformed epithelial cells. In our present study, we demonstrate that ligand-mediated stimulation causes EphA2 to be internalized and degraded. The mechanism of this response involves ligand-mediated autophosphorylation of EphA2, which promotes an association between EphA2 and the c-Cbl adaptor protein. We also show that c-Cbl promotes stimulation-dependent EphA2 degradation. These findings are important for understanding the causes of EphA2 overexpression in malignant cells and provide a foundation for investigating EphA2 as a potential target for therapeutic intervention.
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