Evidence map›Paper›PMID 29228324›Full record

ArticleNucleic acids research2018

USP9X controls translation efficiency via deubiquitination of eukaryotic translation initiation factor 4A1.

Zengxia Li, Zhao Cheng, Chaerkady Raghothama, Zhaomeng Cui, Kaiyu Liu, Xiaojing Li, Chenxiao Jiang, Wei Jiang, Minjia Tan, Xiaohua Ni and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. 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
1.2field-weighted citation impact, top 20% 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, 32 citations in OpenAlex.

  1. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  2. Covalent inhibition ofiScience · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. PARK2 regulates eIF4B-driven lymphomagenesis.Molecular cancer research : MCR · 2022
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  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

13 authors at 4 institutions in 2 countries.

Zengxia LiKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Zhao ChengKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Chaerkady RaghothamaMcKusick-Nathans Institute of Genetic Medicine and the Department of Biological Chemistry, Johns Hopkins University, Baltimore, MD 21205, USA.
Zhaomeng CuiKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Kaiyu LiuKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Xiaojing LiKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Chenxiao JiangKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Wei JiangKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Minjia TanState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Xiaohua NiKey Laboratory of Reproduction Regulation of NPFPC, SIPPR, IAD, Fudan University, Shanghai 200032, China.
Akhilesh PandeyMcKusick-Nathans Institute of Genetic Medicine and the Department of Biological Chemistry, Johns Hopkins University, Baltimore, MD 21205, USA.
Jun O LiuDepartment of Pharmacology & Molecular Sciences and Department of Oncology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Yongjun DangKey Laboratory of Molecular Medicine, Ministry of Education and Department of Biochemistry and Molecular Biology, Shanghai Medical College & Department of Pulmonary and Critical Care Medicine, Huashan Hospital, Fudan University, Shanghai 200032, China.
Fudan University · CNHuashan Hospital · CNJohns Hopkins University · USChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Controlling translation initiation is an efficient way to regulate gene expression at the post-transcriptional level. However, current knowledge regarding regulatory proteins and their modes of controlling translation initiation is still limited. In this study, we employed tandem affinity purification and mass spectrometry to screen for unknown proteins associated with the translation initiation machinery. Ubiquitin specific peptidase 9, X-linked (USP9X), was identified as a novel binding partner, that interacts with the eukaryotic translation initiation factor 4B (eIF4B) in a mRNA-independent manner. USP9X-deficient cells presented significantly impaired nascent protein synthesis, cap-dependent translation initiation and cellular proliferation. USP9X can selectively alter the translation of pro-oncogenic mRNAs, such as c-Myc and XIAP. Moreover, we found that eIF4A1, which is primarily ubiquitinated at Lys-369, is the substrate of USP9X. USP9X dysfunction increases the ubiquitination of eIF4A1 and enhances its degradation. Our results provide evidence that USP9X is a novel regulator of the translation initiation process via deubiquitination of eIF4A1, which offers new insight in understanding the pivotal role of USP9X in human malignancies and neurodevelopmental disorders.

Indexed as

Protein BiosynthesisUbiquitinationCell ProliferationEukaryotic Initiation Factor-4AEukaryotic Initiation FactorsHEK293 CellsHeLa CellsHumansMCF-7 CellsMutationProtein BindingRNA InterferenceRNA, MessengerSubstrate SpecificityUbiquitin ThiolesteraseeIF-4BEukaryotic Initiation Factor-4AEukaryotic Initiation FactorsRNA, MessengerUbiquitin ThiolesteraseUSP9X protein, human

Identifiers

PMID29228324
PMCPMC5778534
OpenAlexW2774520422

What OpenQuestion holds

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LicenceCC BY-NC
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.