期刊
EMBO REPORTS
卷 4, 期 3, 页码 313-319出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/sj.embor.embor767
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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.
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