Evidence map›Paper›PMID 30365499›Full record

ArticlePLoS genetics2018

Filamentation of asparagine synthetase in Saccharomyces cerevisiae.

Shanshan Zhang, Kang Ding, Qing-Ji Shen, Suwen Zhao, Ji-Long Liu

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

26 citing papers in PubMed, 44 citations in OpenAlex.

  1. Chemical reviews · 2026
    Review
  2. Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026
    Review
  3. Review
  4. Article
  5. Cytoophidium complexes resonate with cell fates.Cellular and molecular life sciences : CMLS · 2025
    Article
  6. Article
  7. The Impact of Developmental and Metabolic Cues on Cytoophidium Formation.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Article
  10. CTP synthase: the hissing of the cellular serpent.Histochemistry and cell biology · 2022
    Review
  11. Super-Resolution Imaging Reveals Dynamic Reticular Cytoophidia.International journal of molecular sciences · 2022
    Article
  12. Article
  13. Article
  14. Structural basis for the helical filament formation of Escherichia coli glutamine synthetase.Protein science : a publication of the Protein Society · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Widespread remodeling of proteome solubility in response to different protein homeostasis stresses.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

5 authors at 3 institutions in 2 countries.

Shanshan ZhangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Kang DingSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Qing-Ji ShenMRC Functional Genomics Unit, Department of Physiology, Anatomy and Genetics, University of Oxford, Oxford, United Kingdom.
Suwen ZhaoSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.
Ji-Long LiuSchool of Life Science and Technology, ShanghaiTech University, Shanghai, China.ORCID 0000-0002-4834-8554
ShanghaiTech University · CNChinese Academy of Sciences · CNUniversity of Oxford · GB

Funding

Medical Research Council MC_U137788471Medical Research Council MC_UU_12021/3
6 · The paper itself

Abstract

Asparagine synthetase (ASNS) and CTP synthase (CTPS) are two metabolic enzymes crucial for glutamine homeostasis. A genome-wide screening in Saccharomyces cerevisiae reveal that both ASNS and CTPS form filamentous structures termed cytoophidia. Although CTPS cytoophidia were well documented in recent years, the filamentation of ASNS is less studied. Using the budding yeast as a model system, here we confirm that two ASNS proteins, Asn1 and Asn2, are capable of forming cytoophidia in diauxic and stationary phases. We find that glucose deprivation induces ASNS filament formation. Although ASNS and CTPS form distinct cytoophidia with different lengths, both structures locate adjacently to each other in most cells. Moreover, we demonstrate that the Asn1 cytoophidia colocalize with the Asn2 cytoophidia, while Asn2 filament assembly is largely dependent on Asn1. In addition, we are able to alter Asn1 filamentation by mutagenizing key sites on the dimer interface. Finally, we show that ASN1D330V promotes filamentation. The ASN1D330V mutation impedes cell growth in an ASN2 knockout background, while growing normally in an ASN2 wild-type background. Together, this study reveals a connection between ASNS and CTPS cytoophidia and the differential filament-forming capability between two ASNS paralogs.

Indexed as

AsparagineAspartate-Ammonia LigaseCarbon-Nitrogen LigasesCell CycleCytoskeletonSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsASN1 protein, S cerevisiaeAsparagineAspartate-Ammonia LigaseCarbon-Nitrogen LigasesCTP synthetaseSaccharomyces cerevisiae Proteins

Identifiers

PMID30365499
PMCPMC6221361
OpenAlexW2898235041

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.