MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24

Takayoshi Yamauchi, Masaaki Nishiyama, Toshiro Moroishi, Kanae Yumimoto, Keiichi I. Nakayama

研究成果: ジャーナルへの寄稿学術誌査読

16 被引用数 (Scopus)

抄録

MDM2 mediates the ubiquitylation and thereby triggers the proteasomal degradation of the tumor suppressor protein p53. However, genetic evidence suggests that MDM2 contributes to multiple regulatory networks independently of p53 degradation. We have now identified the DEAD-box RNA helicase DDX24 as a nucleolar protein that interacts with MDM2. DDX24 was found to bind to the central region of MDM2, resulting in the polyubiquitylation of DDX24 both in vitro and in vivo. Unexpectedly, however, the polyubiquitylation of DDX24 did not elicit its proteasomal degradation but rather promoted its association with preribosomal ribonucleoprotein (pre-rRNP) processing complexes that are required for the early steps of pre-rRNA processing. Consistently with these findings, depletion of DDX24 in cells impaired pre-rRNA processing and resulted both in abrogation of MDM2 function and in consequent p53 stabilization. Our results thus suggest an unexpected role of MDM2 in the nonproteolytic ubiquitylation of DDX24, which may contribute to the regulation of pre-rRNA processing.

本文言語英語
ページ(範囲)3321-3340
ページ数20
ジャーナルMolecular and cellular biology
34
17
DOI
出版ステータス出版済み - 2014

!!!All Science Journal Classification (ASJC) codes

  • 分子生物学
  • 細胞生物学

フィンガープリント

「MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル