Evidence map›Paper›PMID 30201806›Full record

ArticleMolecular and cellular biology2018

RACK1 Specifically Regulates Translation through Its Binding to Ribosomes.

Simone Gallo, Sara Ricciardi, Nicola Manfrini, Elisa Pesce, Stefania Oliveto, Piera Calamita, Marilena Mancino, Elisa Maffioli, Monica Moro, Mariacristina Crosti and 4 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

46 citing papers in PubMed, 75 citations in OpenAlex.

  1. A B1 SINE element within the mouseScience advances · 2026
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  2. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
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  3. Structural basis for emetine inhibition of ribosome translocation inbioRxiv : the preprint server for biology · 2026
    Article
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  6. Science advances · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 1 country.

Simone GalloMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy gallo@ingm.org biffo@ingm.org.
Sara RicciardiMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Nicola ManfriniMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Elisa PesceTranslational Research Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Stefania OlivetoMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Piera CalamitaMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Marilena MancinoMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Elisa MaffioliFilarete Foundation, Milan, Italy.
Monica MoroFlow Cytometry Facility, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Mariacristina CrostiFlow Cytometry Facility, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Valeria BernoImaging Facility, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Mauro BombaciProtein Array Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy.
Gabriella TedeschiFilarete Foundation, Milan, Italy.
Stefano BiffoMolecular Histology and Cell Growth Unit, National Institute of Molecular Genetics Romeo e Enrica Invernizzi (INGM), Milan, Italy gallo@ingm.org biffo@ingm.org.
Istituto Nazionale Genetica Molecolare · ITUniversity of Milan · ITFondazione Filarete · ITVita-Salute San Raffaele University · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The translational capability of ribosomes deprived of specific nonfundamental ribosomal proteins may be altered. Physiological mechanisms are scanty, and it is unclear whether free ribosomal proteins can cross talk with the signaling machinery. RACK1 (receptor for activated C kinase 1) is a highly conserved scaffold protein, located on the 40S subunit near the mRNA exit channel. RACK1 is involved in a variety of intracellular contexts, both on and off the ribosomes, acting as a receptor for proteins in signaling, such as the protein kinase C (PKC) family. Here we show that the binding of RACK1 to ribosomes is essential for full translation of capped mRNAs and efficient recruitment of eukaryotic initiation factor 4E (eIF4E).

Indexed as

cell signalingeIF4EeIF6mRNAPKCpuromycinRACK1ribosomesstresstranslational control

Identifiers

PMID30201806
PMCPMC6234289
OpenAlexW2892108787

What OpenQuestion holds

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LicenceCC BY
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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.