Evidence map›Paper›PMID 24665361›Full record

ArticleJournal of extracellular vesicles2014

The endocytosis gene END3 is essential for the glucose-induced rapid decline of small vesicles in the extracellular fraction in Saccharomyces cerevisiae.

Bennett J Giardina, Kathryn Stein, Hui-Ling Chiang

Open access · goldAbstract read
In one paragraph

Article in Journal of extracellular vesicles, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Article
  6. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    Review
  7. Extracellular Vesicles in the Fungi Kingdom.International journal of molecular sciences · 2021
    Review
  8. Review
  9. Article
  10. Article
  11. Extracellular Vesicles From the Cotton PathogenFrontiers in plant science · 2019
    Article
  12. Article
  13. Review
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

3 authors at 1 institution in 1 country.

Bennett J GiardinaDepartment of Cellular and Molecular Physiology, Penn State University College of Medicine, Hershey, PA, USA.
Kathryn SteinDepartment of Cellular and Molecular Physiology, Penn State University College of Medicine, Hershey, PA, USA.
Hui-Ling ChiangDepartment of Cellular and Molecular Physiology, Penn State University College of Medicine, Hershey, PA, USA.
Penn State Milton S. Hershey Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein secretion is a fundamental process in all living cells. Gluconeogenic enzymes are secreted when Saccharomyces cerevisiae are grown in media containing low glucose. However, when cells are transferred to media containing high glucose, they are internalized. We investigated whether or not gluconeogenic enzymes were associated with extracellular vesicles in glucose-starved cells. We also examined the role that the endocytosis gene END3 plays in the internalization of extracellular proteins/vesicles in response to glucose addition.

methodsTransmission electron microscopy was performed to determine the presence of extracellular vesicles in glucose-starved wild-type cells and the dynamics of vesicle transport in cells lacking the END3 gene. Proteomics was used to identify extracellular proteins that associated with these vesicles.

resultsTotal extracts prepared from glucose-starved cells consisted of about 95% small vesicles (30-50 nm) and 5% large structures (100-300 nm). The addition of glucose caused a rapid decline in small extracellular vesicles in wild-type cells. However, most of the extracellular vesicles were still observed in cells lacking the END3 gene following glucose replenishment. Proteomics was used to identify 72 extracellular proteins that may be associated with these vesicles. Gluconeogenic enzymes fructose-1,6-bisphosphatase, malate dehydrogenase, isocitrate lyase, and phosphoenolpyruvate carboxykinase, as well as non-gluconeogenic enzymes glyceraldehyde-3-phosphate dehydrogenase and cyclophilin A, were distributed in the vesicle-enriched fraction in total extracts prepared from cells grown in low glucose. Distribution of these proteins in the vesicle-enriched fraction required the integrity of the membranes. When glucose was added to glucose-starved wild-type cells, levels of extracellular fructose-1,6-bisphosphatase, malate dehydrogenase, isocitrate lyase, phosphoenolpyruvate carboxykinase, glyceraldehyde-3-phosphate dehydrogenase, and cyclophilin A were reduced. In contrast, in cells lacking the END3 gene, levels of these proteins in the extracellular fraction remained high.

conclusionThe END3 gene is required for the rapid decline of extracellular proteins and vesicles in response to glucose addition.

Indexed as

catabolite Inactivationcyclophilin Aextracellular vesiclesfructose-1,6-bisphosphataseglyceraldehyde-3-phosphate dehydrogenaseisocitrate lyasemalate dehydrogenasephosphoenolpyruvate carboxykinasevacuole import and degradation

Identifiers

PMID24665361
PMCPMC3963178
OpenAlexW2052439947

What OpenQuestion 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 OpenQuestion graph.