Autophosphorylation of the insulin-like growth factor I receptor cytoplasmic domain

被引：24
|
作者：
Lopaczynski, W [1 ]
Terry, C [1 ]
Nissley, P [1 ]
机构：
[1] NCI, Metab Branch, NIH, Bethesda, MD 20892 USA
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 279卷 / 03期
基金：
美国国家卫生研究院;
关键词：
6-His tag; insulin receptor; IGF-I receptor dimer;
D O I：
10.1006/bbrc.2000.4046
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The cytoplasmic domain of the beta subunit of the insulin-like growth factor I receptor (amino acids 936-1337) was overexpressed in Sf9 insect cells using a baculovirus expression system, and the g-His tagged receptor was purified by metal-affinity chromatography. Autophosphorylation of the receptor was concentration dependent, consistent with a trans phosphorylation mechanism, Phosphoamino acid analysis of the autophosphorylated receptor showed predominantly phosphotyrosine, but phosphoserine and phosphothreonine were also present. However, when the receptor was further purified by gel filtration on Sephadex G-100 and then autophosphorylated, phosphoaminoacid analysis showed only phosphotyrosine, We conclude that the IGF-I receptor tyrosine kinase is not a dual-specificity kinase and that autophosphorylation of the beta subunit is by a trans mechanism.
引用
收藏
页码：955 / 960
页数：6
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