Insulin receptor substrate-1 (IRS-1) forms a ribonucleoprotein complex associated with polysomes
Insulin receptor substrate-1 (IRS-1) forms a ribonucleoprotein complex associated with polysomes
复制标题
DOI：
10.1016/j.febslet.2013.05.066
复制
发表时间：
2013-08-02
期刊：
影响因子：
3.5
通讯作者：
Takahashi, Shin-Ichiro
中科院分区：
文献类型：
--
作者：
Ozoe, Atsufumi;Sone, Meri;Takahashi, Shin-Ichiro
胰岛素受体底物（insulin receptor substrates，IRSs）在介导细胞内胰岛素样生长因子（insulin-like growth factors，IGFs）/胰岛素信号转导中起重要作用。在这项研究中，我们确定了信使核糖核蛋白（mRNP）作为IRS-1相关蛋白的组成部分。IRS-1复合物形成分析表明，IRS-1被纳入分子量超过1000 kDa的复合物中，这些复合物被RNase处理破坏。此外，oligo（dT）珠从细胞裂解物中沉淀IRS-1，表明IRS-1复合物含有信使RNA。结合IRS-1被分离成含有多核糖体的高密度组分的数据，我们认为IRS-1与mRNP形成了新的复合物。蛋白质相互作用的结构概述：IRS-1通过抗诱饵免疫共沉淀与PABPC-1发生物理相互作用（查看交互：1,2）IRS 1通过抗标签免疫共沉淀与PABPC 1物理相互作用（查看相互作用）IRS 1通过抗诱饵免疫共沉淀与PABPC 1发生物理相互作用IRS 1通过抗诱饵免疫共沉淀与EIF 4F和PABPC 1发生物理相互作用（查看互动）（C）2013年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Insulin receptor substrates (IRSs) are known to play important roles in mediating intracellular insulin-like growth factors (IGFs)/insulin signaling. In this study, we identified components of messenger ribonucleoprotein (mRNP) as IRS-1-associated proteins. IRS-1 complex formation analysis revealed that IRS-1 is incorporated into the complexes of molecular mass more than 1000 kDa, which were disrupted by treatment with RNase. Furthermore, oligo(dT) beads precipitated IRS-1 from cell lysates, showing that the IRS-1 complexes contained messenger RNA. Taken together with the data that IRS-1 was fractionated into the polysome-containing high-density fractions, we concluded that IRS-1 forms the novel complexes with mRNPs.Structured summary of protein interactions:IRS1 physically interacts with PABPC1 by anti bait coimmunoprecipitation (View Interaction: 1,2)IRS1 physically interacts with PABPC1 by anti tag coimmunoprecipitation (View interaction)IRS1 physically interacts with PABPC1 by anti bait coimmunoprecipitation (View interaction)IRS1 physically interacts with EIF4F and PABPC1 by anti bait coimmunoprecipitation (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.