Evidence map›Paper›PMID 36848233›Full record

ArticleCell reports2023

SAYSD1 senses UFMylated ribosome to safeguard co-translational protein translocation at the endoplasmic reticulum.

Lihui Wang, Yue Xu, Sijung Yun, Quan Yuan, Prasanna Satpute-Krishnan, Yihong Ye

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Review
  3. The mechanistic basis and cellular functions of UFMylation.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. UFMylation promotes orthoflavivirus infectious particle production.bioRxiv : the preprint server for biology · 2025
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article
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

6 authors at 2 institutions in 1 country.

Lihui WangLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Yue XuLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Sijung YunLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Quan YuanDendrite Morphogenesis and Plasticity Unit, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Prasanna Satpute-KrishnanDepartment of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, MD 20814, USA.
Yihong YeLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: yihongy@mail.nih.gov.
National Institutes of Health · USUniformed Services University of the Health Sciences · US

Funding

Study dendrite morphogenesis and activity-dependent plasticity using DrosophilaZIANS003137 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI YUAN, QUAN · 2013 to 2025
$24.9M
Mechanism of protein retro-translocation from the endoplasmic reticulumZIADK033008 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI YE, YIHONG · 2010 to 2025
$9.3M
The Mechanistic Basis of Selective ER-Export of Misfolded Secretory Pathway ProteinsR01GM134327 · NIGMS · HENRY M. JACKSON FDN FOR THE ADV MIL/MED · PI SATPUTE-KRISHNAN, PRASANNA · 2019 to 2023
$1.6M
Intramural NIH HHS ZIA DK033008NIGMS NIH HHS R01 GM134327
6 · The paper itself

Abstract

Translocon clogging at the endoplasmic reticulum (ER) as a result of translation stalling triggers ribosome UFMylation, activating translocation-associated quality control (TAQC) to degrade clogged substrates. How cells sense ribosome UFMylation to initiate TAQC is unclear. We conduct a genome-wide CRISPR-Cas9 screen to identify an uncharacterized membrane protein named SAYSD1 that facilitates TAQC. SAYSD1 associates with the Sec61 translocon and also recognizes both ribosome and UFM1 directly, engaging a stalled nascent chain to ensure its transport via the TRAPP complex to lysosomes for degradation. Like UFM1 deficiency, SAYSD1 depletion causes the accumulation of translocation-stalled proteins at the ER and triggers ER stress. Importantly, disrupting UFM1- and SAYSD1-dependent TAQC in Drosophila leads to intracellular accumulation of translocation-stalled collagens, defective collagen deposition, abnormal basement membranes, and reduced stress tolerance. Thus, SAYSD1 acts as a UFM1 sensor that collaborates with ribosome UFMylation at the site of clogged translocon, safeguarding ER homeostasis during animal development.

Indexed as

Drosophila ProteinsEndoplasmic ReticulumRibosomesAnimalsBasement MembraneDrosophilaFenbendazoleMembrane ProteinsProtein TransportDrosophila ProteinsFenbendazoleMembrane Proteinscollagen biogenesisco-translational protein translocationCP: Molecular biologyDrosophilaribosome stalling/translation arrestSAYSD1Sec61translocation-associated quality control/TAQCtranslocon cloggingUFM1/UFMylation

Identifiers

PMID36848233
PMCPMC10010011
OpenAlexW4317756907

What Socratic 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 Socratic graph.