Evidence map›Paper›PMID 37036982›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum.

Francesco Scavone, Samantha C Gumbin, Paul A Da Rosa, Ron R Kopito

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
10.5field-weighted citation impact, top 1% 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, 68 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. The mechanistic basis and cellular functions of UFMylation.Nature reviews. Molecular cell biology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism.bioRxiv : the preprint server for biology · 2026
    Article
  13. Article
  14. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  15. Review
  16. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Francesco ScavoneDepartment of Biology, Stanford University, Stanford, CA 94305.ORCID 0000-0003-3560-7120
Samantha C GumbinDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.ORCID 0000-0002-0257-509X
Paul A Da RosaDepartment of Biology, Stanford University, Stanford, CA 94305.
Ron R KopitoDepartment of Biology, Stanford University, Stanford, CA 94305.
Stanford University · US

Funding

Supplement to Enhance Wellness and Resiliency in the Graduate EnvironmentT32GM007276 · NIGMS · STANFORD UNIVERSITY · PI MORRISON, ASHBY J. · 1985 to 2023
$32.9M
The Ubiquitin Proteasome System in Quality ControlR01GM074874 · NIGMS · STANFORD UNIVERSITY · PI KOPITO, RON R · 2006 to 2022
$8.0M
The role of UFMylation in ribosome quality control at the ERR01GM148477 · NIGMS · STANFORD UNIVERSITY · PI RON R KOPITO · 2023 to 2026
$2.4M
NIGMS NIH HHS R01 GM074874NIGMS NIH HHS R01 GM148477NIGMS NIH HHS T32 GM007276
6 · The paper itself

Abstract

Ribosomes that stall while translating cytosolic proteins are incapacitated by incomplete nascent chains, termed "arrest peptides" (APs) that are destroyed by the ubiquitin proteasome system (UPS) via a process known as the ribosome-associated quality control (RQC) pathway. By contrast, APs on ribosomes that stall while translocating secretory proteins into the endoplasmic reticulum (ER-APs) are shielded from cytosol by the ER membrane and the tightly sealed ribosome-translocon junction (RTJ). How this junction is breached to enable access of cytosolic UPS machinery and 26S proteasomes to translocon- and ribosome-obstructing ER-APs is not known. Here, we show that UPS and RQC-dependent degradation of ER-APs strictly requires conjugation of the ubiquitin-like (Ubl) protein UFM1 to 60S ribosomal subunits at the RTJ. Therefore, UFMylation of translocon-bound 60S subunits modulates the RTJ to promote access of proteasomes and RQC machinery to ER-APs.

Indexed as

Endoplasmic ReticulumRibosomesQuality ControlRibosomal ProteinsUbiquitinsRibosomal ProteinsUbiquitinsendoplasmic reticulumribosome-associated quality controlubiquitinUFM1UFMylation

Identifiers

PMID37036982
PMCPMC10120006
OpenAlexW4363677338

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.