Evidence map›Paper›PMID 22753847›Full record

ArticleEukaryotic cell2012

Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion.

Natsuko Miura, Aya Kirino, Satoshi Endo, Hironobu Morisaka, Kouichi Kuroda, Masahiro Takagi, Mitsuyoshi Ueda

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Surface enolase is a virulence factor ofFrontiers in microbiology · 2026
    Article
  3. Endocytic tethers modulate unconventional GAPDH secretion.Cell surface (Amsterdam, Netherlands) · 2025
    Article
  4. Promising immunotherapeutic targets for treating candidiasis.Frontiers in cellular and infection microbiology · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Through the back door: Unconventional protein secretion.Cell surface (Amsterdam, Netherlands) · 2020
    Review
  12. Article
  13. Article
  14. Review
  15. Frontiers in physiology · 2019
    Article
  16. Review
  17. Article
  18. From plasminogen to plasmin: role of plasminogen receptors in human cancer.International journal of molecular sciences · 2014
    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

7 authors at 4 institutions in 1 country.

Natsuko MiuraDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, Japan.
Aya Kirino
Satoshi Endo
Hironobu Morisaka
Kouichi Kuroda
Masahiro Takagi
Mitsuyoshi Ueda
Kyoto University · JPJapan Advanced Institute of Science and Technology · JPJapan Society for the Promotion of Science · JPKyoto Municipal Institute of Industrial Technology and Culture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycolytic enzymes are cytosolic proteins, but they also play important extracellular roles in cell-cell communication and infection. We used Saccharomyces cerevisiae to analyze the secretory pathway of some of these enzymes, including enolase, phosphoglucose isomerase, triose phosphate isomerase, and fructose 1,6-bisphosphate aldolase. Enolase, phosphoglucose isomerase, and an N-terminal 28-amino-acid-long fragment of enolase were secreted in a sec23-independent manner. The enhanced green fluorescent protein (EGFP)-conjugated enolase fragment formed cellular foci, some of which were found at the cell periphery. Therefore, we speculated that an overview of the secretory pathway could be gained by investigating the colocalization of the enolase fragment with intracellular proteins. The DsRed-conjugated enolase fragment colocalized with membrane proteins at the cis-Golgi complex, nucleus, endosome, and plasma membrane, but not the mitochondria. In addition, the secretion of full-length enolase was inhibited in a knockout mutant of the intracellular SNARE protein-coding gene TLG2. Our results suggest that enolase is secreted via a SNARE-dependent secretory pathway in S. cerevisiae.

Indexed as

Cell MembraneEndosomesGenes, ReporterGlucose-6-Phosphate IsomeraseGolgi ApparatusGreen Fluorescent ProteinsLuminescent ProteinsMitochondriaMutationPhosphopyruvate HydrataseProtein TransportQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory Pathwayenolase 2, S cerevisiaefluorescent protein 583Glucose-6-Phosphate IsomeraseGreen Fluorescent ProteinsLuminescent ProteinsPhosphopyruvate HydrataseQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsTLG2 protein, S cerevisiae

Identifiers

PMID22753847
PMCPMC3416056
OpenAlexW2160829255

What OpenQuestion holds

Textmetadata
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.