Evidence map›Paper›PMID 22771119›Full record

ArticleMolecular cell2012

Protection of extraribosomal RPL13a by GAPDH and dysregulation by S-nitrosylation.

Jie Jia, Abul Arif, Belinda Willard, Jonathan D Smith, Dennis J Stuehr, Stanley L Hazen, Paul L Fox

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Malonate promotes CD8Cellular & molecular immunology · 2025
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Jie JiaDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.
Abul Arif
Belinda Willard
Jonathan D Smith
Dennis J Stuehr
Stanley L Hazen
Paul L Fox
Cleveland Clinic Lerner College of Medicine · US

Funding

Clinical and Translational Science Collaborative of ClevelandUL1TR000439 · NCATS · CASE WESTERN RESERVE UNIVERSITY · PI KONSTAN, MICHAEL W. · 2012 to 2016
$50.0M
Vascular Cell function and AtherosclerosisP01HL029582 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI LI, XIAOXIA · 1985 to 2019
$32.0M
Structural Determinants Of Ceruloplasmin Inflammatory ActivityP01HL076491 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI GOGONEA, VALENTIN · 2004 to 2019
$27.3M
A protein-directed RNA switch that regulates translationR01GM086430 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI FOX, PAUL L · 2009 to 2016
$2.6M
NCATS NIH HHS UL1 TR000439NHLBI NIH HHS P01 HL029582NHLBI NIH HHS P01 HL076491NIGMS NIH HHS R01 GM086430
6 · The paper itself

Abstract

Multiple eukaryotic ribosomal proteins (RPs) are co-opted for extraribosomal "moonlighting" activities, but paradoxically, RPs exhibit rapid turnover when not ribosome-bound. In one illustrative case of a functional extraribosomal RP, interferon (IFN)-γ induces ribosome release of L13a and assembly into the IFN-gamma-activated inhibitor of translation (GAIT) complex for translational control of a subset of inflammation-related proteins. Here we show GAPDH functions as a chaperone, shielding newly released L13a from proteasomal degradation. However, GAPDH protective activity is lost following cell treatment with oxidatively modified low density lipoprotein and IFN-γ. These agonists stimulate S-nitrosylation at Cys(247) of GAPDH, which fails to interact with L13a, causing proteasomal degradation of essentially the entire cell complement of L13a and defective translational control. Evolution of extraribosomal RP activities might require coevolution of protective chaperones, and pathological disruption of either protein, or their interaction, presents an alternative mechanism of diseases due to RP defects, and targets for therapeutic intervention.

Indexed as

GaitGene SilencingHumansInterferon-gammaLipoproteins, LDLMolecular ChaperonesMyeloid CellsPhosphorylationProteasome Endopeptidase ComplexProtein BindingProtein BiosynthesisRibosomal ProteinsRibosomesU937 CellsVascular Endothelial Growth Factor AInterferon-gammaLipoproteins, LDLMolecular ChaperonesProteasome Endopeptidase ComplexRibosomal ProteinsRPL13A protein, humanVascular Endothelial Growth Factor AVEGFA protein, human

Identifiers

PMID22771119
PMCPMC3635105
OpenAlexW1999921207

What OpenQuestion 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 OpenQuestion graph.