SIRT7 deacetylates DDB1 and suppresses the activity of the CRL4 E3 ligase complexes
文献类型：期刊论文
| 作者 | Mo, Yan2,3; Lin, Ran2,3; Liu, Peng2,3; Tan, Minjia4,5 ; Xiong, Yue2,3,6; Guan, Kun-Liang1,2,3,7; Yuan, Hai-Xin2,3
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| 刊名 | FEBS JOURNAL
 |
| 出版日期 | 2017-11 |
| 卷号 | 284期号:21页码:3619-3636 |
| 关键词 | acetylation CRL4 E3 ligase DDB1 nucleolar function inhibition SIRT7 |
| ISSN号 | 1742-464X |
| DOI | 10.1111/febs.14264 |
| 文献子类 | Article |
| 英文摘要 | Cullin 4 (CUL4) and small ring finger protein ROC1 assemble to form E3 ubiquitin ligase (CRL4) complexes. CUL4 interacts with WD-40 proteins through the adaptor protein DNA damage-binding protein 1 (DDB1) to target substrates for ubiquitylation. Very little is known on how the CUL4 and DDB1 interaction is regulated. Here, we show that DDB1 is acetylated and acetylation promotes DDB1 binding to CUL4. We also identify nucleolar sirtuin 7 (SIRT7) as a major deacetylase that negatively regulates DDB1-CUL4 interaction. Following inhibition of nucleolar function by actinomycin D or 5-fluorouracil treatment or knocking down the gene for the RNA polymerase I component UBF, SIRT7 is mobilized from the nucleolus to the nucleoplasm and promotes DDB1 deacetylation, leading to decreased DDB1-CUL4 association and CRL4 activity. This results in the accumulation or activation of CRL4 substrates including LATS1 and p73, which contribute to cell apoptosis induced by actinomycin D and 5-fluorouracil. Our study uncovers a novel regulation of CRL4 E3 ligase complexes. |
| WOS关键词 | RNA-POLYMERASE-I ; UBIQUITIN-PROTEASOME PATHWAY ; CDK INHIBITOR P27 ; NUCLEOLAR STRESS ; RIBOSOME BIOGENESIS ; COP9 SIGNALOSOME ; HIPPO PATHWAY ; DEGRADATION ; APOPTOSIS ; PROTEIN |
| 资助项目 | National Key Research and Development Program of China[2016YFA0501800] ; National Natural Science Foundation of China[31570784] ; National Natural Science Foundation of China[81372198] ; National Natural Science Foundation of China[81522033] |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000414918100006 |
| 出版者 | WILEY |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/272421]  |
| 专题 | 化学蛋白质组学研究中心 中科院受体结构与功能重点实验室 新药研究国家重点实验室 |
| 通讯作者 | Yuan, Hai-Xin |
| 作者单位 | 1.Univ Calif San Diego, Dept Pharmacol, La Jolla, CA 92093 USA; 2.Fudan Univ, Inst Biomed Sci, Peoples Hosp Shanghai 5, Shanghai 20032, Peoples R China; 3.Fudan Univ, Inst Biomed Sci, Mol & Cell Biol Res Lab, Shanghai 20032, Peoples R China; 4.Chinese Acad Sci, Shanghai Inst Mat Med, Chem Prote Ctr, Shanghai, Peoples R China; 5.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai, Peoples R China; 6.Univ N Carolina, Lineberger Comprehens Canc Ctr, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA; 7.Univ Calif San Diego, Moores Canc Ctr, La Jolla, CA 92093 USA |
| 推荐引用方式 GB/T 7714 | Mo, Yan,Lin, Ran,Liu, Peng,et al. SIRT7 deacetylates DDB1 and suppresses the activity of the CRL4 E3 ligase complexes[J]. FEBS JOURNAL,2017,284(21):3619-3636. |
| APA | Mo, Yan.,Lin, Ran.,Liu, Peng.,Tan, Minjia.,Xiong, Yue.,...&Yuan, Hai-Xin.(2017).SIRT7 deacetylates DDB1 and suppresses the activity of the CRL4 E3 ligase complexes.FEBS JOURNAL,284(21),3619-3636. |
| MLA | Mo, Yan,et al."SIRT7 deacetylates DDB1 and suppresses the activity of the CRL4 E3 ligase complexes".FEBS JOURNAL 284.21(2017):3619-3636. |
入库方式： OAI收割
来源：上海药物研究所
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