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The phosphorylation status of nuclear rpS3 is reciprocally regulated by PKCdelta and PP2A

阿平添加于 2009-5-24 16:24 | 2221 次阅读 | 0 个评论

作者
Kim TS, Kim HD, Shin HS, Kim J
摘要
It has been previously shown that ribosomal protein S3 (rpS3) has an endonuclease activity which is increased by PKCdelta-dependent phosphorylation. However, the reciprocal mechanism for rpS3 dephosphorylation is not known. In this study, we examined phosphatases involved in rpS3 dephosphorylation and determined that rpS3 is specifically dephosphorylated by PP2A. By immunoprecipitation assay, rpS3 only interacted with PP2Ac, but not with PP1. The interaction between rpS3 and PP2Ac occurred only in the nuclear fraction. Moreover, the PP2Ac association with rpS3 was identified in cells transfected with wild-type rpS3, but not with mutant rpS3 lacking PKCdelta phosphorylation sites. PP2A inhibition using okadaic acid induced rpS3 phosphorylation. The level of phosphorylated rpS3 in cells was decreased by the overexpression of PP2Ac and was increased by the downregulation of PP2Ac. Taken together, these results suggest that oxidative stress regulates the phosphorylation status of non-ribosomal rpS3 by both activating PKCdelta and blocking the PP2A interaction with rpS3.
详细资料
- 文献种类: Journal Article
- 期刊名称: The Journal of Biological Chemistry
- 期刊缩写: J Biol Chem
- 期卷页: 2009年
- 地址: Korea University, Korea, Republic of
- ISBN: 0021-9258
- 备注:PMID:19458393
学科领域生物医药 » 生物学
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PP2A rpS3
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