Evidence map›Paper›PMID 34871442›Full record

ArticleNucleic acids research2021

Phosphorylation of ribosomal protein S6 differentially affects mRNA translation based on ORF length.

Jonathan Bohlen, Mykola Roiuk, Aurelio A Teleman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
4.1field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 68 citations in OpenAlex.

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  8. Targeting enhancing myelin regeneration reverses cognitive deficits in a mouse model of intellectual disability.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026
    Article
  9. PHGDH is a targetable driver of PDAC progression.bioRxiv : the preprint server for biology · 2026
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  17. Neuronal processes contain the essential components for the late steps of ribosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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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

3 authors at 1 institution in 1 country.

Jonathan BohlenGerman Cancer Research Center (DKFZ), 69120 Heidelberg, Germany.
Mykola RoiukGerman Cancer Research Center (DKFZ), 69120 Heidelberg, Germany.
Aurelio A TelemanGerman Cancer Research Center (DKFZ), 69120 Heidelberg, Germany.ORCID 0000-0002-4237-9368
German Cancer Research Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation of Ribosomal Protein S6 (RPS6) was the first post-translational modification of the ribosome to be identified and is a commonly-used readout for mTORC1 activity. Although the cellular and organismal functions of RPS6 phosphorylation are known, the molecular consequences of RPS6 phosphorylation on translation are less well understood. Here we use selective ribosome footprinting to analyze the location of ribosomes containing phosphorylated RPS6 on endogenous mRNAs in cells. We find that RPS6 becomes progressively dephosphorylated on ribosomes as they translate an mRNA. As a consequence, average RPS6 phosphorylation is higher on mRNAs with short coding sequences (CDSs) compared to mRNAs with long CDSs. We test whether RPS6 phosphorylation differentially affects mRNA translation based on CDS length by genetic removal of RPS6 phosphorylation. We find that RPS6 phosphorylation promotes translation of mRNAs with short CDSs more strongly than mRNAs with long CDSs. Interestingly, RPS6 phosphorylation does not promote translation of mRNAs with 5' TOP motifs despite their short CDS lengths, suggesting they are translated via a different mode. In sum this provides a dynamic view of RPS6 phosphorylation on ribosomes as they translate mRNAs and the functional consequence on translation.

Indexed as

Protein BiosynthesisAnimalsCells, CulturedHeLa CellsHumansImmunoblottingMechanistic Target of Rapamycin Complex 1MiceMutationOpen Reading FramesPhosphorylationProtein Processing, Post-TranslationalRibosomal Protein S6RibosomesRNA, MessengerRNA-SeqMechanistic Target of Rapamycin Complex 1Ribosomal Protein S6RNA, Messenger

Identifiers

PMID34871442
PMCPMC8682771
OpenAlexW4226395114

What OpenQuestion holds

Textmetadata
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.