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FEBS Lett. 2000 Mar 17;470(1):15-9.

Termination of IL-6-induced STAT activation is independent of receptor internalization but requires de novo protein synthesis.

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Institute of Biochemistry, Rheinisch-Westfälische Technische Hochschule Aachen, Pauwelsstr. 30, 52057, Aachen, Germany.


The interleukin-6 (IL-6) receptor complex comprises the IL-6 receptor (IL-6R, gp80) and the signal transducer gp130. Binding of IL-6 to its receptor results in dimerization of gp130, activation of the Jak/STAT pathway, and in a down-regulation of IL-6 binding sites by endocytosis. The STAT activation after stimulation is transient, being maximal after 15-30 min and disappearing after 60-90 min. The mechanism which leads to the termination of the signal is still unknown. In this paper we have studied whether the down-modulation of the STAT signal requires the endocytosis of the receptor complex. Our results suggest that the desensitization of the IL-6 signal is not due to internalization of the receptor complex but requires de novo protein synthesis.

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