Dynamics of the interaction between the insulin receptor and protein tyrosine-phosphatase 1B in living cells

被引：89

作者：

Boute, N ^{[1
]}

Boubekeur, S ^{[1
]}

Lacasa, D ^{[1
]}

Issad, T ^{[1
]}

机构：

[1] Univ Paris 05, Dept Biol, Inst Cochin, CNRS,UMR 8104,INSERM,U567, F-75014 Paris, France

来源：

EMBO REPORTS | 2003年 / 4卷 / 03期

关键词：

D O I：

10.1038/sj.embor.embor767

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 dynamics of the interaction of the insulin receptor with a substrate-trapping mutant of protein-tyrosine phosphatase 1 B (PTP1 B) were monitored in living human embryonic kidney cells using bioluminescence resonance energy transfer (BRET). Insulin dose-dependently stimulates this interaction, which could be followed in real time for more than 30 minutes. The effect of insulin on the BRET signal could be detected at early time-points (30 seconds), suggesting that in intact cells the tyrosine-kinase activity of the insulin receptor is tightly controlled by PTP1 B. Interestingly, the basal (insulin-independent) interaction of the insulin receptor with PTP1 B was much weaker with a soluble form of the tyrosine-phosphatase than with the endoplasmic reticulum (ER)-targeted form. Inhibition of insulin-receptor processing using tunicamycin suggests that the basal interaction occurs during insulin-receptor biosynthesis in the ER. Therefore, localization of PTP1 B in this compartment might be important for the regulation of insulin receptors during their biosynthesis.

引用

页码：313 / 319

页数：7

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