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激酶结构域内第845密码子处一个高度保守的酪氨酸残基对于人表皮生长因子受体的转化活性并非必需。

A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor.

作者信息

Gotoh N, Tojo A, Hino M, Yazaki Y, Shibuya M

机构信息

Department of Genetics, University of Tokyo, Japan.

出版信息

Biochem Biophys Res Commun. 1992 Jul 31;186(2):768-74. doi: 10.1016/0006-291x(92)90812-y.

DOI:10.1016/0006-291x(92)90812-y
PMID:1323290
Abstract

Epidermal growth factor receptor (EGF-R) is a widely expressed ligand-dependent tyrosine kinase. The tyrosine residue at 845 in EGF-R corresponds to Y416 of v/c-src kinase, which is highly conserved and functionally important in many tyrosine kinases. To clarify the functional role of Y845, we constructed a mutant human EGF-R in which this tyrosine was replaced with phenylalanine and transfected it to NIH3T3 cells. EGF-R F845 induced EGF-dependent cellular transformation and revealed tyrosine-autophosphorylation of a 170 kDa protein, and initiated DNA synthesis similar to the wild-type EGF-R. We conclude here that Y845 is dispensable in the above mentioned functions of EGF-R tyrosine kinase.

摘要

表皮生长因子受体(EGF-R)是一种广泛表达的依赖配体的酪氨酸激酶。EGF-R中845位的酪氨酸残基对应于v/c-src激酶的Y416,在许多酪氨酸激酶中高度保守且功能重要。为阐明Y845的功能作用,我们构建了一个将该酪氨酸替换为苯丙氨酸的突变型人EGF-R,并将其转染至NIH3T3细胞。EGF-R F845诱导了依赖EGF的细胞转化,显示出170 kDa蛋白的酪氨酸自磷酸化,并启动了与野生型EGF-R相似的DNA合成。我们在此得出结论,Y845在EGF-R酪氨酸激酶的上述功能中是不必要的。

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