PPM1G 可使 eIF4E 去磷酸化，从而控制 mRNA 翻译和细胞增殖。

IF 3.3 2区生物学 Q1 BIOLOGY Life Science Alliance Pub Date : 2024-08-07 Print Date: 2024-10-01 DOI:10.26508/lsa.202402755

Peng Wang, Zixian Li, Sung-Hoon Kim, Haijin Xu, Hao Huang, Chutong Yang, Abby Snape, Jung-Hyun Choi, Sara Bermudez, Marie-Noelle Boivin, Nicolas Ferry, Jason Karamchandani, Bhushan Nagar, Nahum Sonenberg

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引用次数: 0

摘要

mRNA 5'cap 结合真核翻译起始因子 4E (eIF4E)在控制健康和疾病中的 mRNA 翻译方面发挥着关键作用。调控 eIF4E 活性的机制之一是通过 MNK 激酶对 eIF4E 进行磷酸化，从而促进编码促肿瘤蛋白的一组 mRNA 的翻译。有关 eIF4E 磷酸化酶的研究一直很少。在这里，我们发现 PPM1G 是使 eIF4E 去磷酸化的磷酸酶。我们描述了 PPM1G 中的 eIF4E 结合基序，它与 4E 结合蛋白（4E-BPs）相似。我们证明了 PPM1G 可通过靶向磷酸化 eIF4E 依赖性 mRNA 翻译来抑制细胞增殖。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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PPM1G dephosphorylates eIF4E in control of mRNA translation and cell proliferation.

The mRNA 5'cap-binding eukaryotic translation initiation factor 4E (eIF4E) plays a critical role in the control of mRNA translation in health and disease. One mechanism of regulation of eIF4E activity is via phosphorylation of eIF4E by MNK kinases, which promotes the translation of a subset of mRNAs encoding pro-tumorigenic proteins. Work on eIF4E phosphatases has been paltry. Here, we show that PPM1G is the phosphatase that dephosphorylates eIF4E. We describe the eIF4E-binding motif in PPM1G that is similar to 4E-binding proteins (4E-BPs). We demonstrate that PPM1G inhibits cell proliferation by targeting phospho-eIF4E-dependent mRNA translation.

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来源期刊

Life Science Alliance Agricultural and Biological Sciences-Plant Science

CiteScore

5.80

自引率

2.30%

发文量

241

审稿时长

10 weeks

期刊介绍： Life Science Alliance is a global, open-access, editorially independent, and peer-reviewed journal launched by an alliance of EMBO Press, Rockefeller University Press, and Cold Spring Harbor Laboratory Press. Life Science Alliance is committed to rapid, fair, and transparent publication of valuable research from across all areas in the life sciences.