Evidence map›Paper›PMID 27117520›Full record

ArticleeLife2016

The ribosomal protein Asc1/RACK1 is required for efficient translation of short mRNAs.

Mary K Thompson, Maria F Rojas-Duran, Paritosh Gangaramani, Wendy V Gilbert

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed, 1 pooled it
9.4field-weighted citation impact, top 2% 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

94 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.

  1. Pooled it
  2. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
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  5. Science advances · 2026
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  8. Review
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  10. Review
  11. Specialized ribosomes: integrating new insights and current challenges.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Review
  12. Article
  13. Review
  14. High-resolution reconstruction of aRNA (New York, N.Y.) · 2024
    Article
  15. Article
  16. Ribosome Assembly and Repair.Annual review of cell and developmental biology · 2024
    Review
  17. Review
  18. Article
  19. Article
  20. Article

34 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Mary K ThompsonDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0002-4947-6048
Maria F Rojas-DuranDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.
Paritosh GangaramaniDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0002-4893-8167
Wendy V GilbertDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United States.ORCID 0000-0003-2807-9657
Eunice Kennedy Shriver National Institute of Child Health and Human Development · US

Funding

PRE-DOCTORAL TRAINING IN THE BIOLOGICAL SCIENCEST32GM007287 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BELL, STEPHEN P., KEATING, AMY E · 1985 to 2019
$40.8M
Ribosome Specialization and RegulationR01GM094303 · NIGMS · YALE UNIVERSITY · PI GILBERT, WENDY VICTORIA · 2012 to 2016
$1.5M
NIGMS NIH HHS R01 GM094303NIGMS NIH HHS T32 GM007287
6 · The paper itself

Abstract

Translation is a core cellular process carried out by a highly conserved macromolecular machine, the ribosome. There has been remarkable evolutionary adaptation of this machine through the addition of eukaryote-specific ribosomal proteins whose individual effects on ribosome function are largely unknown. Here we show that eukaryote-specific Asc1/RACK1 is required for efficient translation of mRNAs with short open reading frames that show greater than average translational efficiency in diverse eukaryotes. ASC1 mutants in S. cerevisiae display compromised translation of specific functional groups, including cytoplasmic and mitochondrial ribosomal proteins, and display cellular phenotypes consistent with their gene-specific translation defects. Asc1-sensitive mRNAs are preferentially associated with the translational 'closed loop' complex comprised of eIF4E, eIF4G, and Pab1, and depletion of eIF4G mimics the translational defects of ASC1 mutants. Together our results reveal a role for Asc1/RACK1 in a length-dependent initiation mechanism optimized for efficient translation of genes with important housekeeping functions.

Indexed as

Protein BiosynthesisAdaptor Proteins, Signal TransducingGene DeletionGTP-Binding ProteinsRibosomal ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingASC1 protein, S cerevisiaeGTP-Binding ProteinsRibosomal ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsAsc1biochemistryRACK1ribosomeS. cerevisiaetranslation

Identifiers

PMID27117520
PMCPMC4848094
OpenAlexW2342962008

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.