Roles of mTOR and JNK in serine phosphorylation, translocation, and degradation of IRS-1
Roles of mTOR and JNK in serine phosphorylation, translocation, and degradation of IRS-1
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DOI：
10.1016/j.bbrc.2005.07.152
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发表时间：
2005-09-30
影响因子：
3.1
通讯作者：
Kobayashi, M
中科院分区：
文献类型：
--
作者：
Hiratani, K;Haruta, T;Kobayashi, M
在3T3-L1脂肪细胞中，胰岛素或山奈素可促进IRS-1在Ser(307)和Ser(636/639)处的磷酸化，这两种作用均可被mTOR抑制剂雷帕霉素或JNK抑制剂SP600125部分抑制，并可被两者联合使用进一步抑制。有趣的是，SP600125降低了苯甲霉素诱导的p70(S6K)的磷酸化，而不降低胰岛素诱导的p70(S6K)的磷酸化。此外，与胰岛素不同的是，茴香霉素不能引起IRS-1的易位或降解。这些结果表明，mTOR和JNK在IRS-1丝氨酸残基的磷酸化过程中起作用，而胰岛素和茴香素在mTOR和JNK之间的激活关系以及对IRS-1定位和稳定性的影响方面是不同的。(C)2005 Elsevier Inc.保留所有权利。
In 3T3-L1 adipocytes, insulin or anisomycin stimulated phosphorylation of IRS-1 at Ser(307) and Ser(636/639), both of which were partially reduced by the mTOR inhibitor, rapamycin, or the JNK inhibitor, SP600125, and were further inhibited by a combination of them. Interestingly, anisomycin-induced p70(S6K) phosphorylation was reduced by SP600125, while insulin-induced p70(S6K) phosphorylation was not. Furthermore, unlike insulin, anisomycin failed to elicit translocation or degradation of IRS-1. These results indicate that mTOR and JNK play roles in phosphorylating IRS-1 serine residues, and that insulin and anisomycin are different in terms of the relationship of activation between mTOR and JNK, and the effects on IRS-1 localization and stability. (C) 2005 Elsevier Inc. All rights reserved.