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ERK1/ERK2和p70S6K信号通路在蛋白质合成的胰岛素信号传导中的作用。

Role of ERK1/ERK2 and p70S6K pathway in insulin signalling of protein synthesis.

作者信息

Sale E M, Atkinson P P, Arnott C H, Chad J E, Sale G J

机构信息

Division of Biochemistry and Molecular Biology, School of Biological Sciences, Southampton, UK.

出版信息

FEBS Lett. 1999 Mar 5;446(1):122-6. doi: 10.1016/s0014-5793(99)00193-3.

Abstract

The signalling pathways by which insulin triggers protein synthesis were studied using an antisense strategy to deplete ERK1/ERK2 and rapamycin to inhibit the p70S6K pathway. The results indicated that ERK1/ERK2 principally regulated the amount of the protein synthesis machinery available in the cell while the p70S6K pathway contributed to modulating its activation in response to insulin. ERK1/ERK2 also mediated in a small proportion of insulin-stimulated protein synthesis which included the induction of c-fos protein. When c-fos induction was blocked the majority of insulin-stimulated protein synthesis still occurred and thus did not require transcriptional regulation of c-fos or its targets.

摘要

利用反义策略去除细胞外调节蛋白激酶1/2(ERK1/ERK2)以及使用雷帕霉素抑制p70核糖体蛋白S6激酶(p70S6K)信号通路,对胰岛素触发蛋白质合成的信号通路进行了研究。结果表明,ERK1/ERK2主要调节细胞内可用的蛋白质合成机制的数量,而p70S6K信号通路则有助于调节其对胰岛素的反应激活。ERK1/ERK2也介导了一小部分胰岛素刺激的蛋白质合成,其中包括c-fos蛋白的诱导。当c-fos诱导被阻断时,大部分胰岛素刺激的蛋白质合成仍然发生,因此不需要c-fos或其靶标的转录调控。

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