Evidence map›Paper›PMID 24980433›Full record

ArticleMolecular and cellular biology2014

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

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

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.4field-weighted citation impact, top 34% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. DEAD Box Helicase 24 Is Increased in the Brain in Alzheimer's Disease andInternational journal of molecular sciences · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Takayoshi YamauchiDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Fukuoka, and CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama, Japan.
Masaaki NishiyamaDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Fukuoka, and CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama, Japan.
Toshiro MoroishiDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Fukuoka, and CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama, Japan.
Kanae YumimotoDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Fukuoka, and CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama, Japan.
Keiichi I NakayamaDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Higashi-ku, Fukuoka, Fukuoka, and CREST, Japan Science and Technology Agency (JST), Kawaguchi, Saitama, Japan nakayak1@bioreg.kyushu-u.ac.jp.
Kyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Amino Acid SequenceConserved SequenceDEAD-box RNA HelicasesHCT116 CellsHumansMolecular Sequence DataMultiprotein ComplexesNuclear ProteinsProteasome Endopeptidase ComplexProtein Interaction Domains and MotifsProtein StabilityProteolysisProto-Oncogene Proteins c-mdm2RibonucleoproteinsRNA PrecursorsRNA Processing, Post-TranscriptionalDDX24 protein, humanDEAD-box RNA HelicasesMDM2 protein, humanMultiprotein ComplexesNIP7 protein, humanNuclear ProteinsProteasome Endopeptidase ComplexProto-Oncogene Proteins c-mdm2RibonucleoproteinsRNA PrecursorsTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID24980433
PMCPMC4135551
OpenAlexW2128063923

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.