Evidence map›Paper›PMID 38363833›Full record

ArticleScience advances2024

Distinct roles of LARP1 and 4EBP1/2 in regulating translation and stability of 5'TOP mRNAs.

Tobias Hochstoeger, Panagiotis Papasaikas, Ewa Piskadlo, Jeffrey A Chao

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Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

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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

4 authors.

Tobias HochstoegerFriedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.ORCID 0000-0002-8061-7857
Panagiotis PapasaikasFriedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.ORCID 0000-0002-1640-7636
Ewa PiskadloFriedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.
Jeffrey A ChaoFriedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.ORCID 0000-0002-5895-9156

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A central mechanism of mTOR complex 1 (mTORC1) signaling is the coordinated translation of ribosomal protein and translation factor mRNAs mediated by the 5'-terminal oligopyrimidine motif (5'TOP). Recently, La-related protein 1 (LARP1) was proposed to be the specific regulator of 5'TOP mRNA translation downstream of mTORC1, while eIF4E-binding proteins (4EBP1/2) were suggested to have a general role in translational repression of all transcripts. Here, we use single-molecule translation site imaging of 5'TOP and canonical mRNAs to study the translation of single mRNAs in living cells. Our data reveal that 4EBP1/2 has a dominant role in repression of translation of both 5'TOP and canonical mRNAs during pharmacological inhibition of mTOR. In contrast, we find that LARP1 selectively protects 5'TOP mRNAs from degradation in a transcriptome-wide analysis of mRNA half-lives. Our results clarify the roles of 4EBP1/2 and LARP1 in regulating 5'TOP mRNAs and provide a framework to further study how these factors control cell growth during development and disease.

Indexed as

Protein BiosynthesisTOR Serine-Threonine KinasesMechanistic Target of Rapamycin Complex 1RNA, MessengerSignal TransductionMechanistic Target of Rapamycin Complex 1RNA, MessengerTOR Serine-Threonine Kinases

Identifiers

PMID38363833
PMCPMC10871529

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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.