PKCδ-dependent functional switch of rpS3 between translation and DNA repair
PKCδ-dependent functional switch of rpS3 between translation and DNA repair
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DOI：
10.1016/j.bbamcr.2008.10.017
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发表时间：
2009-02-01
影响因子：
5.1
通讯作者：
Kim, Joon
中科院分区：
文献类型：
--
作者：
Kim, Tae-Sung;Kim, Hag Dong;Kim, Joon
核糖体蛋白S3（rpS3）作为核糖体40S亚基的一个组成部分，在翻译中起关键作用，并参与DNA损伤的处理，作为损伤DNA内切酶发挥作用。然而，目前还不清楚rpS3的功能如何在翻译和DNA修复之间切换。在这里，我们表明，PKC δ磷酸化rpS3导致其在细胞核中的动员，以修复受损的DNA。磷酸化的rpS3仅在非核糖体rpS3中检测到，并且rpS3的修复内切酶活性通过其磷酸化而增加。此外，rpS3敲低细胞表现出更敏感的基因毒性应激比对照细胞，这种敏感性被纠正过表达的野生型rpS3，但不是磷酸化缺陷的rpS3。总之，我们认为rpS3分子在翻译和DNA修复之间的命运是由PKC δ依赖性磷酸化调节的。(c)2008 Elsevier B.V.保留所有权利。
Ribosomal protein S3 (rpS3) is critically involved in translation as a component of the 40S ribosomal subunit and participates in the processing of DNA damage, functioning as a damage DNA endonuclease. However, it is not yet known how the function of rpS3 switches between translation and DNA repair. Here we show that PKC delta phosphorylates rpS3 resulting in its mobilization in the nucleus to repair damaged DNA. Phosphorylated rpS3 was only detected in non-ribosomal rpS3 and the repair endonuclease activity of rpS3 was increased by its phosphorylation. In addition, rpS3 knock-down cells showed more sensitivity to genotoxic stress than control cells, and this sensitivity was corrected by overexpressed wild-type rpS3 but not by phosphorylation defective rpS3. In conclusion, we propose that the destiny of rpS3 molecules between translation and DNA repair is regulated by PKC delta-dependent phosphorylation. (c) 2008 Elsevier B.V. All rights reserved.