Evidence map›Paper›PMID 31729466›Full record

ArticleCell research2019

Cryo-EM structure of SMG1-SMG8-SMG9 complex.

Li Zhu, Liang Li, Yilun Qi, Zishuo Yu, Yanhui Xu

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Making PI3K superfamily enzymes run faster.Advances in biological regulation · 2025
    Review
  8. Article
  9. Review
  10. Article
  11. Protein model refinement for cryo-EM maps using AlphaFold2 and the DAQ score.Acta crystallographica. Section D, Structural biology · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Suppression of Nonsense Mutations by New Emerging Technologies.International journal of molecular sciences · 2020
    Review
  20. 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.

Li Zhu *Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Key Laboratory of Medical Epigenetics and Metabolism, Shanghai Medical College of Fudan University, Shanghai, 200032, China.
Liang Li *Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Key Laboratory of Medical Epigenetics and Metabolism, Shanghai Medical College of Fudan University, Shanghai, 200032, China.
Yilun Qi *Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Key Laboratory of Medical Epigenetics and Metabolism, Shanghai Medical College of Fudan University, Shanghai, 200032, China.
Zishuo YuFudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Key Laboratory of Medical Epigenetics and Metabolism, Shanghai Medical College of Fudan University, Shanghai, 200032, China.
Yanhui XuFudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Key Laboratory of Medical Epigenetics and Metabolism, Shanghai Medical College of Fudan University, Shanghai, 200032, China. xuyh@fudan.edu.cn.ORCID http://orcid.org/0000-0002-1408-5178
Shanghai Medical College of Fudan University · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31821002National Natural Science Foundation of China (National Science Foundation of China) 31830107
6 · The paper itself

Abstract

Nonsense-mediated mRNA decay (NMD) targets premature stop codon (PTC)-containing mRNAs for rapid degradation, and is essential for mammalian embryonic development, brain development and modulation of the stress response. The key event in NMD is the SMG1-mediated phosphorylation of an RNA helicase UPF1 and SMG1 kinase activity is inhibited by SMG8 and SMG9 in an unknown mechanism. Here, we determined the cryo-EM structures of human SMG1 at 3.6 Å resolution and the SMG1-SMG8-SMG9 complex at 3.4 Å resolution, respectively. SMG8 has a C-terminal kinase inhibitory domain (KID), which covers the catalytic pocket and inhibits the kinase activity of SMG1. Structural analyses suggest that GTP hydrolysis of SMG9 would lead to a dramatic conformational change of SMG8-SMG9 and the KID would move away from the inhibitory position to restore SMG1 kinase activity. Thus, our structural and biochemical analyses provide a mechanistic understanding of SMG1-SMG8-SMG9 complex assembly and the regulatory mechanism of SMG1 kinase activity.

Indexed as

Cryoelectron MicroscopyHumansIntracellular Signaling Peptides and ProteinsModels, MolecularNonsense Mediated mRNA DecayPhosphorylationProtein BindingProtein ConformationProtein KinasesProtein Serine-Threonine KinasesRNA HelicasesTrans-ActivatorsIntracellular Signaling Peptides and ProteinsProtein KinasesProtein Serine-Threonine KinasesRNA HelicasesSMG1 protein, humanSMG8 protein, humanSMG9 protein, humanTrans-ActivatorsUPF1 protein, human

Identifiers

PMID31729466
PMCPMC6951342
OpenAlexW2988598871

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.