2018年12月
Novel ubiquitin-independent nucleolar c-Myc degradation pathway mediated by antizyme 2
Scientific Reports
- ,
- ,
- ,
- 巻
- 8
- 号
- 1
- 開始ページ
- 3005
- 終了ページ
- 3005
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/s41598-018-21189-0
- 出版者・発行元
- Springer Science and Business Media LLC
The proto-oncogene c-Myc encodes a short-lived protein c-Myc that regulates various cellular processes including cell growth, differentiation and apoptosis. Degradation of c-Myc is catalyzed by the proteasome and requires phosphorylation of Thr-58 for ubiquitination by E3 ubiquitin ligase, Fbxw7/ FBW7. Here we show that a polyamine regulatory protein, antizyme 2 (AZ2), interacts with c-Myc in the nucleus and nucleolus, to accelerate proteasome-mediated c-Myc degradation without ubiquitination or Thr-58 phosphorylation. Polyamines, the inducer of AZ2, also destabilize c-Myc in an AZ2-dependent manner. Knockdown of AZ2 by small interfering RNA (siRNA) increases nucleolar c-Myc and also cellular pre-rRNA whose synthesis is promoted by c-Myc. AZ2-dependent c-Myc degradation likely operates under specific conditions such as glucose deprivation or hypoxia. These findings reveal the targeting mechanism for nucleolar ubiquitin-independent c-Myc degradation.
- リンク情報
- ID情報
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- DOI : 10.1038/s41598-018-21189-0
- ISSN : 2045-2322
- eISSN : 2045-2322
- PubMed ID : 29445227
- PubMed Central 記事ID : PMC5813005
- SCOPUS ID : 85042087167