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学科主题: 临床医学
题名:
Phosphorylation of Pirh2 by Calmodulin-dependent kinase II impairs its ability to ubiquitinate p53
作者: Duan, Shanshan; Yao, Zhan; Hou, Dezhi; Wu, Zhengsheng; Zhu, Wei-Guo; Wu, Mian
关键词: CaMK II ; p53 ; phosphorylation ; Pirh2 ; ubiquitination
刊名: EMBO JOURNAL
发表日期: 2007-07-11
DOI: 10.1038/sj.emboj.7601749
卷: 26, 期:13, 页:3062-3074
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Biochemistry & Molecular Biology ; Cell Biology
研究领域[WOS]: Biochemistry & Molecular Biology ; Cell Biology
关键词[WOS]: PROTEIN LIGASE ; CELLS ; APOPTOSIS ; ACTIVATION ; EXPRESSION ; MDM2 ; LOCALIZATION ; MODULATION ; DEATH ; GENE
英文摘要:

Although the recently identified Pirh2 protein is known as a p53-induced ubiquitin-protein E3 ligase, which negatively regulates p53, the detailed mechanism underlying the regulation of Pirh2 remains largely unknown. Here, we demonstrate that while Pirh2 is mostly detected in the phosphorylated form in normal tissues, it is predominantly present in the unphosphorylated form in majority of tumor cell lines and tissues examined. Phosphorylated Pirh2 is far more unstable than its unphosphorylated form. We further identified that Calmodulin-dependent kinase II (CaMK II) phosphorylates Pirh2 on residues Thr-154 and Ser-155. Phosphorylation of Pirh2 appears to be regulated through cell cycle-dependent mechanism. CaMK II-mediated Pirh2 phosphorylation abrogates its E3 ligase activity toward p53. Together, our data suggest that phosphorylation of Pirh2 may act as a fine-tuning to maintain the balance of p53-Pirh2 autoregulatory feedback loop, which facilitates the tight regulation of p53 stability and tumor suppression.

语种: 英语
WOS记录号: WOS:000248038500003
Citation statistics:
内容类型: 期刊论文
URI标识: http://ir.bjmu.edu.cn/handle/400002259/56774
Appears in Collections:北京大学临床肿瘤学院_期刊论文

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作者单位: 1.Anhui Med Univ, Dept Pathol, Hefei, Peoples R China
2.Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Phys Sci Microsale, Hefei 230027, Peoples R China
3.Peking Univ, Hlth Sci Ctr, Canc Res Ctr, Dept Biochem & Mol Biol, Beijing, Peoples R China

Recommended Citation:
Duan, Shanshan,Yao, Zhan,Hou, Dezhi,et al. Phosphorylation of Pirh2 by Calmodulin-dependent kinase II impairs its ability to ubiquitinate p53[J]. EMBO JOURNAL,2007,26(13):3062-3074.
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