Evidence map›Paper›PMID 28673543›Full record

ArticleMolecular cell2017

Autogenous Control of 5′TOP mRNA Stability by 40S Ribosomes.

Antonio Gentilella, Francisco D Morón-Duran, Pedro Fuentes, Guilherme Zweig-Rocha, Ferran Riaño-Canalias, Joffrey Pelletier, Marta Ruiz, Gemma Turón, Julio Castaño, Albert Tauler and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
4.8field-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

87 citing papers in PubMed, 126 citations in OpenAlex.

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  10. Translational Downregulation of 5' TOP mRNAs During T Cell Exhaustion.bioRxiv : the preprint server for biology · 2025
    Article
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27 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

14 authors at 4 institutions in 2 countries.

Antonio GentilellaMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain; Department of Biochemistry and Physiology, Faculty of Pharmacy, Universitat de Barcelona, 08028 Barcelona, Spain. Electronic address: agentilella@idibell.cat.
Francisco D Morón-DuranMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Pedro FuentesMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Guilherme Zweig-RochaMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Ferran Riaño-CanaliasMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Joffrey PelletierMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Marta RuizMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Gemma TurónMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain.
Julio CastañoDivision of Hematology/Oncology, Department of Internal Medicine, University of Cincinnati Medical School, Cincinnati, OH 45267-0508, USA.
Albert TaulerMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain; Department of Biochemistry and Physiology, Faculty of Pharmacy, Universitat de Barcelona, 08028 Barcelona, Spain.
Clara BuenoJosep Carreras Leukemia Research Institute and School of Medicine, University of Barcelona, 08916 Barcelona, Spain.
Pablo MenéndezJosep Carreras Leukemia Research Institute and School of Medicine, University of Barcelona, 08916 Barcelona, Spain; Institut Catala de Recerca i Estudis Avançats (ICREA) Lluis Companys, 08916 Barcelona, Spain.
Sara C KozmaMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain; Division of Hematology/Oncology, Department of Internal Medicine, University of Cincinnati Medical School, Cincinnati, OH 45267-0508, USA.
George ThomasMetabolism and Cancer Group, Molecular Mechanisms And Experimental Therapy In Oncology Program, Bellvitge Biomedical Research Institute, IDIBELL, 08908 Barcelona, Spain; Division of Hematology/Oncology, Department of Internal Medicine, University of Cincinnati Medical School, Cincinnati, OH 45267-0508, USA; Physiological Sciences Department, Faculty of Medicine and Health Science, University of Barcelona, 08908 Barcelona, Spain. Electronic address: gthomas@idibell.cat.
Institut d'Investigació Biomédica de Bellvitge · ESUniversitat de Barcelona · ESUniversity of Cincinnati · USJosep Carreras Leukaemia Research Institute · ES

Funding

The Function of rpL5 and rpL11 in induction of p53R01CA158768 · NCI · UNIVERSITY OF CINCINNATI · PI THOMAS, GEORGE · 2012 to 2017
$1.5M
NCI NIH HHS R01 CA158768
6 · The paper itself

Abstract

Ribosomal protein (RP) expression in higher eukaryotes is regulated translationally through the 5′TOP sequence. This mechanism evolved to more rapidly produce RPs on demand in different tissues. Here we show that 40S ribosomes, in a complex with the mRNA binding protein LARP1, selectively stabilize 5′TOP mRNAs, with disruption of this complex leading to induction of the impaired ribosome biogenesis checkpoint (IRBC) and p53 stabilization. The importance of this mechanism is underscored in 5q− syndrome, a macrocytic anemia caused by a large monoallelic deletion, which we found to also encompass the LARP1 gene. Critically, depletion of LARP1 alone in human adult CD34+ bone marrow precursor cells leads to a reduction in 5′TOP mRNAs and the induction of p53. These studies identify a 40S ribosome function independent of those in translation that, with LARP1, mediates the autogenous control of 5′TOP mRNA stability, whose disruption is implicated in the pathophysiology of 5q− syndrome.

Indexed as

Protein BiosynthesisRNA 5' Terminal Oligopyrimidine SequenceRNA StabilityAnemia, MacrocyticAutoantigensBone Marrow CellsChromosome DeletionChromosomes, Human, Pair 5HCT116 CellsHumansMultiprotein ComplexesProtein BindingRibonucleoproteinsRibosomal ProteinsRibosomesRNA InterferenceAutoantigensMultiprotein ComplexesRibonucleoproteinsribosomal protein L11ribosomal protein L5, humanRibosomal ProteinsRNA, MessengerSS-B AntigenTP53 protein, humanTumor Suppressor Protein p5340S ribosomes5q(?) syndrome5?TOP mRNAsimpaired ribosome biogenesis checkpointp53 stabilizationpolysome profilesribosomal proteins

Identifiers

PMID28673543
PMCPMC5553558
OpenAlexW2733653638

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.