作者: Lifeng Feng , Jin-Tao Wang , Hongchuan Jin , Kaixian Qian , Jian-Guo Geng
DOI: 10.1002/CBF.1792
关键词:
摘要: The binding of Cbl-interacting protein 85 kDa (CIN85) to c-Cbl is important endocytosis and degradation epidermal growth factor receptor (EGFR). proline-arginine motif PXXXPR in SH3 domains CIN85 are essential this interaction. Here we demonstrated that SH3KBP1 1 (SHKBP1), which also contains two motifs, constitutively bound CIN85. Importantly, the SHKBP1 prevented interaction with inhibited translocation EGFR containing vesicles, thus reducing enhancing EGF induced SRE transcription activity. Therefore, our results indicated could promote signaling pathway by interrupting c-Cbl-CIN85 complex inhibiting degradation.