Evidence map›Paper›PMID 39533057›Full record

ArticleThe EMBO journal2024

LARP1 binds ribosomes and TOP mRNAs in repressed complexes.

James A Saba, Zixuan Huang, Kate L Schole, Xianwen Ye, Shrey D Bhatt, Yi Li, Winston Timp, Jingdong Cheng, Rachel Green

Abstract read
In one paragraph

Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. eLife · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Translational Downregulation of 5' TOP mRNAs During T Cell Exhaustion.bioRxiv : the preprint server for biology · 2025
    Article
  10. Article
  11. Article
  12. Article
  13. Biomolecular NMR assignments · 2025
    Article
  14. Article
  15. Article
  16. Conserved Functions of LARP1 Proteins in Eukaryotes.Wiley interdisciplinary reviews. RNA
    Review
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

9 authors.

James A Saba *Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.ORCID http://orcid.org/0000-0003-3453-8151
Zixuan Huang *Minhang Hospital & Institutes of Biomedical Sciences, Shanghai Key Laboratory of Medical Epigenetics, International Co-laboratory of Medical Epigenetics and Metabolism, Fudan University, Dong'an Road 131, 200032, Shanghai, China.ORCID http://orcid.org/0000-0001-6483-6606
Kate L ScholeDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Xianwen YeMinhang Hospital & Institutes of Biomedical Sciences, Shanghai Key Laboratory of Medical Epigenetics, International Co-laboratory of Medical Epigenetics and Metabolism, Fudan University, Dong'an Road 131, 200032, Shanghai, China.
Shrey D BhattDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Yi LiMinhang Hospital & Institutes of Biomedical Sciences, Shanghai Key Laboratory of Medical Epigenetics, International Co-laboratory of Medical Epigenetics and Metabolism, Fudan University, Dong'an Road 131, 200032, Shanghai, China.
Winston TimpDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Jingdong ChengMinhang Hospital & Institutes of Biomedical Sciences, Shanghai Key Laboratory of Medical Epigenetics, International Co-laboratory of Medical Epigenetics and Metabolism, Fudan University, Dong'an Road 131, 200032, Shanghai, China. cheng@fudan.edu.cn.ORCID http://orcid.org/0000-0003-4442-377X
Rachel GreenDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA. ragreen@jhmi.edu.ORCID http://orcid.org/0000-0001-9337-2003

Funding

Medical Scientist Training ProgramT32GM136577 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ANDREA L COX · 2020 to 2026
$13.4M
Direct nanopore detection of modified RNA to probe structure and dynamicsR01HG010538 · NHGRI · JOHNS HOPKINS UNIVERSITY · PI TIMP, WINSTON GEORGE · 2019 to 2022
$3.1M
Defining protein synthesis demands and specificities in multiple myelomaF30CA260910 · NCI · JOHNS HOPKINS UNIVERSITY · PI SABA, JAMES ANDREW · 2021 to 2023
$155k
HHS | NIH | National Cancer Institute (NCI) F30CA260910HHS | NIH | National Human Genome Research Institute (NHGRI) HG010538HHS | NIH | National Institute of General Medical Sciences (NIGMS) T32GM136577Howard Hughes Medical Institute (HHMI) HHMI_GREENNational Key R & D Program of China 2023YFC2413204National Natural Science Foundation of China 32371350NCI NIH HHS F30 CA260910NHGRI NIH HHS R01 HG010538NIGMS NIH HHS T32 GM136577Shanghai Municipal Science and Technology Commission 22410712400Shanghai Municipal Science and Technology Commission 22ZR1413600
6 · The paper itself

Abstract

Terminal oligopyrimidine motif-containing mRNAs (TOPs) encode all ribosomal proteins in mammals and are regulated to tune ribosome synthesis to cell state. Previous studies have implicated LARP1 in 40S- or 80S-ribosome complexes that are thought to repress and stabilize TOPs. However, a molecular understanding of how LARP1 and TOPs interact with these ribosome complexes is lacking. Here, we show that LARP1 directly binds non-translating ribosomal subunits. Cryo-EM structures reveal a previously uncharacterized domain of LARP1 bound to and occluding the mRNA channel of the 40S subunit. Increased availability of free ribosomal subunits downstream of various stresses promote 60S joining at the same interface to form LARP1-80S complexes. Simultaneously, LARP1 engages the TOP via its previously characterized La/PAM2 and DM15 domains. Contrary to expectations, ribosome binding within these complexes is not required for LARP1-mediated TOP repression or stabilization, two canonical LARP1 functions. Together, this work provides molecular insight into how LARP1 directly binds ribosomal subunits and challenges existing models describing the function of repressed LARP1-40S/80S-TOP complexes.

Indexed as

AutoantigensCryoelectron MicroscopyRibonucleoproteinsRNA, MessengerSS-B AntigenHEK293 CellsHumansProtein BindingRibosomal ProteinsRibosomesRNA 5' Terminal Oligopyrimidine SequenceAutoantigensRibonucleoproteinsRibosomal ProteinsRNA, MessengerSS-B AntigenCryo-EMLARP1RibosomeTOP mRNATranslation

Identifiers

PMID39533057
PMCPMC11649897

What Socratic holds

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Registered trials

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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 Socratic graph.