Evidence map›Paper›PMID 28559344›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding.

Richard W P Smith, Ross C Anderson, Osmany Larralde, Joel W S Smith, Barbara Gorgoni, William A Richardson, Poonam Malik, Sheila V Graham, Nicola K Gray

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Seneca Valley virus 3CFrontiers in microbiology · 2023
    Review
  9. Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Seneca Valley Virus 3CPathogens (Basel, Switzerland) · 2020
    Article
  18. Review
  19. The role of CSDE1 in translational reprogramming and human diseases.Cell communication and signaling : CCS · 2020
    Review
  20. Translational Control in Virus-Infected Cells.Cold Spring Harbor perspectives in biology · 2019
    Review
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

9 authors at 3 institutions in 1 country.

Richard W P SmithMedical Research Council Centre for Reproductive Health, Queen's Medical Research Institute, University of Edinburgh, Edinburgh EH16 4TJ, United Kingdom; nicola.gray@ed.ac.uk r.smith@ed.ac.uk.
Ross C AndersonMedical Research Council Centre for Reproductive Health, Queen's Medical Research Institute, University of Edinburgh, Edinburgh EH16 4TJ, United Kingdom.
Osmany LarraldeMedical Research Council-University of Glasgow Centre for Virus Research, Garscube Campus, Glasgow G61 1QH, United Kingdom.
Joel W S SmithMedical Research Council Human Genetics Unit, University of Edinburgh, Western General Hospital, Edinburgh EH4 2XU, United Kingdom.
Barbara GorgoniMedical Research Council Centre for Reproductive Health, Queen's Medical Research Institute, University of Edinburgh, Edinburgh EH16 4TJ, United Kingdom.
William A RichardsonMedical Research Council Centre for Reproductive Health, Queen's Medical Research Institute, University of Edinburgh, Edinburgh EH16 4TJ, United Kingdom.
Poonam MalikMedical Research Council-University of Glasgow Centre for Virus Research, Garscube Campus, Glasgow G61 1QH, United Kingdom.
Sheila V GrahamMedical Research Council-University of Glasgow Centre for Virus Research, Garscube Campus, Glasgow G61 1QH, United Kingdom.
Nicola K GrayMedical Research Council Centre for Reproductive Health, Queen's Medical Research Institute, University of Edinburgh, Edinburgh EH16 4TJ, United Kingdom; nicola.gray@ed.ac.uk r.smith@ed.ac.uk.
Medical Research Council · GBUniversity of Edinburgh · GBWestern General Hospital · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I02137X/1Medical Research Council G117/564Medical Research Council G78/7826Medical Research Council G9826324Medical Research Council MC_U127692697Medical Research Council MC_UU_12014/3Medical Research Council MR/J003069/1Medical Research Council MR/P02419X/1Wellcome TrustWellcome Trust 084359/Z/07/Z
6 · The paper itself

Abstract

Regulation of mRNA translation is a major control point for gene expression and is critical for life. Of central importance is the complex between cap-bound eukaryotic initiation factor 4E (eIF4E), eIF4G, and poly(A) tail-binding protein (PABP) that circularizes mRNAs, promoting translation and stability. This complex is often targeted to regulate overall translation rates, and also by mRNA-specific translational repressors. However, the mechanisms of mRNA-specific translational activation by RNA-binding proteins remain poorly understood. Here, we address this deficit, focusing on a herpes simplex virus-1 protein, ICP27. We reveal a direct interaction with PABP that is sufficient to promote PABP recruitment and necessary for ICP27-mediated activation. PABP binds several translation factors but is primarily considered to activate translation initiation as part of the PABP-eIF4G-eIF4E complex that stimulates the initial cap-binding step. Importantly, we find that ICP27-PABP forms a complex with, and requires the activity of, eIF4G. Surprisingly, ICP27-PABP-eIF4G complexes act independently of the effects of PABP-eIF4G on cap binding to promote small ribosomal subunit recruitment. Moreover, we find that a cellular mRNA-specific regulator, Deleted in Azoospermia-like (Dazl), also employs the PABP-eIF4G interaction in a similar manner. We propose a mechanism whereby diverse RNA-binding proteins directly recruit PABP, in a non-poly(A) tail-dependent manner, to stimulate the small subunit recruitment step. This strategy may be particularly relevant to biological conditions associated with hypoadenylated mRNAs (e.g., germ cells/neurons) and/or limiting cytoplasmic PABP (e.g., viral infection, cell stress). This mechanism adds significant insight into our knowledge of mRNA-specific translational activation and the function of the PABP-eIF4G complex in translation initiation.

Indexed as

AnimalsEukaryotic Initiation Factor-4GFemaleImmediate-Early ProteinsModels, BiologicalMutationOocytesPeptide Chain Initiation, TranslationalPoly(A)-Binding ProteinsProtein BindingRecombinant ProteinsRNA CapsRNA, MessengerRNA, ViralTwo-Hybrid System TechniquesXenopus laevisEukaryotic Initiation Factor-4GICP27 protein, human herpesvirus 1Immediate-Early ProteinsPoly(A)-Binding ProteinsRecombinant ProteinsRNA CapsRNA, MessengerRNA, ViralDAZLICP27mRNA-binding proteinmRNA-specific translational regulationpoly(A)-binding protein

Identifiers

PMID28559344
PMCPMC5474791
OpenAlexW2620392373

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.