Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl
Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl
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DOI：
10.1006/bbrc.2000.2147
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发表时间：
2000-02-16
影响因子：
3.1
通讯作者：
Kajigaya, S
中科院分区：
文献类型：
--
作者：
Take, H;Watanabe, S;Kajigaya, S
c-Cbl原癌基因产物是蛋白酪氨酸激酶的重要底物，在多种细胞表面受体的刺激下迅速被酪氨酸磷酸化。我们鉴定了一种新的c-Cbl相互作用蛋白CIN 85，其分子量为85 kDa，与接头蛋白CMS和CD 2AP相似，CIN 85 mRNA在正常人体组织和分析的癌细胞系中普遍表达。CIN 85与c-Cbl基本相关。对于CIN 85与c-Cbl的相互作用，CIN 85的第二个SH 3结构域显示为中心参与者。CIN 85-c-Cbl协会增强后不久，刺激293细胞与表皮生长因子（EGF），并逐渐减少到基础水平，这与c-Cbl的酪氨酸磷酸化水平。我们的研究结果表明，CIN 85可能通过与c-Cbl的相互作用在EGF受体介导的信号级联中发挥特定的作用。(C)北京大学出版社.
The c-Cbl protooncogene product is a prominent substrate of protein tyrosine kinases and is rapidly tyrosine-phosphorylated upon stimulation of a wide variety of cell-surface receptors, We have identified a novel c-Cbl-interacting protein termed CIN85 with a molecular mass of 85 kDa which shows similarity to adaptor proteins, CMS and CD2AP, CIN85 mRNA is expressed ubiquitously in normal human tissues and cancer cell lines analyzed. CIN85 was basally associated with c-Cbl. For interaction of CIN85 with c-Cbl, the second SH3 domain of CIN85 was shown to serve as a central player. The CIN85-c-Cbl association was enhanced shortly after stimulation of 293 cells with epidermal growth factor (EGF) and gradually diminished to a basal level, which correlated with a tyrosine phosphorylation level of c-Cbl. Our results suggest that CIN85 may play a specific role in the EGF receptor-mediated signaling cascade via its interaction with c-Cbl. (C) 2000 Academic Press.