Evidence map›Paper›PMID 27348078›Full record

ArticleNature structural & molecular biology2016

Neddylation requires glycyl-tRNA synthetase to protect activated E2.

Zhongying Mo, Qian Zhang, Ze Liu, Janelle Lauer, Yi Shi, Litao Sun, Patrick R Griffin, Xiang-Lei Yang

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Association Between Neddylation and Immune Response.Frontiers in cell and developmental biology · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Roles of Aminoacyl-tRNA Synthetases in Cancer.Frontiers in cell and developmental biology · 2020
    Review
  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

8 authors at 1 institution in 1 country.

Zhongying MoDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
Qian ZhangDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
Ze LiuDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
Janelle LauerDepartment of Molecular Therapeutics, The Scripps Research Institute, Jupiter, Florida, USA.
Yi ShiDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
Litao SunDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
Patrick R GriffinDepartment of Molecular Therapeutics, The Scripps Research Institute, Jupiter, Florida, USA.
Xiang-Lei YangDepartment of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.
Scripps Research Institute · US

Funding

Extra-translational roles of aminoacyl tRNA synthetases in connection to diseaseR01GM088278 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI YANG, XIANG-LEI · 2010 to 2019
$3.7M
NIGMS NIH HHS R01 GM088278
6 · The paper itself

Abstract

Neddylation is a post-translational modification that controls the cell cycle and proliferation by conjugating the ubiquitin-like protein NEDD8 to specific targets. Here we report that glycyl-tRNA synthetase (GlyRS), an essential enzyme in protein synthesis, also plays a critical role in neddylation. In human cells, knockdown of GlyRS, but not knockdown of a different tRNA synthetase, decreased the global level of neddylation and caused cell-cycle abnormality. This function of GlyRS is achieved through direct interactions with multiple components of the neddylation pathway, including NEDD8, E1, and E2 (Ubc12). Using various structural and functional approaches, we show that GlyRS binds the APPBP1 subunit of E1 and captures and protects activated E2 (NEDD8-conjugated Ubc12) before the activated E2 reaches a downstream target. Therefore, GlyRS functions as a chaperone that critically supports neddylation. This function is probably conserved in all eukaryotic GlyRS enzymes and may contribute to the strong association of GlyRS with cancer progression.

Indexed as

Breast NeoplasmsCatalytic DomainCell CycleGlycine-tRNA LigaseHEK293 CellsHeLa CellsHumansKaplan-Meier EstimateKineticsNEDD8 ProteinProportional Hazards ModelsProtein BindingProtein Processing, Post-TranslationalProtein StabilityProteolysisUbiquitin-Activating EnzymesGlycine-tRNA LigaseNAE protein, humanNEDD8 ProteinNEDD8 protein, humanUBE2M protein, humanUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesUbiquitins

Identifiers

PMID27348078
PMCPMC4972647
OpenAlexW2465969468

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.