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锌指蛋白ZPR1与表皮生长因子受体的结合。

Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor.

作者信息

Galcheva-Gargova Z, Konstantinov K N, Wu I H, Klier F G, Barrett T, Davis R J

机构信息

Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.

出版信息

Science. 1996 Jun 21;272(5269):1797-802. doi: 10.1126/science.272.5269.1797.

Abstract

ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.

摘要

ZPR1是一种锌指蛋白,可与表皮生长因子受体(EGFR)的细胞质酪氨酸激酶结构域结合。缺失分析表明,这种结合相互作用是由ZPR1的锌指以及EGFR酪氨酸激酶的X和XI亚结构域介导的。用表皮生长因子(EGF)处理哺乳动物细胞会导致ZPR1与EGFR的结合减少,以及ZPR1在细胞核中的积累。EGF调节ZPR1结合的作用取决于EGFR的酪氨酸磷酸化。因此,ZPR1代表了一类与EGFR结合并在激活后从受体上释放的分子的原型。

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