Evidence map›Paper›PMID 16174741›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Distinct functional units of the Golgi complex in Drosophila cells.

Hiroyuki Yano, Miki Yamamoto-Hino, Masato Abe, Reiko Kuwahara, Shuka Haraguchi, Isamu Kusaka, Wakae Awano, Akiko Kinoshita-Toyoda, Hidenao Toyoda, Satoshi Goto

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

46 citing papers in PubMed, 113 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. The Golgi Apparatus and its Next-Door Neighbors.Frontiers in cell and developmental biology · 2022
    Review
  10. Article
  11. Heparan Sulfate Proteoglycan Clustering in Wnt Signaling and Dispersal.Frontiers in cell and developmental biology · 2020
    Review
  12. Review
  13. Editorial: Golgi Dynamics in Physiological and Pathological Conditions.Frontiers in cell and developmental biology · 2020
    Article
  14. Article
  15. Article
  16. The Golgin Protein Giantin Regulates Interconnections Between Golgi Stacks.Frontiers in cell and developmental biology · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. Intracellular Golgi Complex organization reveals tissue specific polarity during zebrafish embryogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2016
    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

10 authors at 2 institutions in 1 country.

Hiroyuki YanoMitsubishi-Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194-8511, Japan.
Miki Yamamoto-Hino
Masato Abe
Reiko Kuwahara
Shuka Haraguchi
Isamu Kusaka
Wakae Awano
Akiko Kinoshita-Toyoda
Hidenao Toyoda
Satoshi Goto
Chiba University · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A striking variety of glycosylation occur in the Golgi complex in a protein-specific manner, but how this diversity and specificity are achieved remains unclear. Here we show that stacked fragments (units) of the Golgi complex dispersed in Drosophila imaginal disk cells are functionally diverse. The UDP-sugar transporter FRINGE-CONNECTION (FRC) is localized to a subset of the Golgi units distinct from those harboring SULFATELESS (SFL), which modifies glucosaminoglycans (GAGs), and from those harboring the protease RHOMBOID (RHO), which processes the glycoprotein SPITZ (SPI). Whereas the glycosylation and function of NOTCH are affected in imaginal disks of frc mutants, those of SPI and of GAG core proteins are not, even though FRC transports a broad range of glycosylation substrates, suggesting that Golgi units containing FRC and those containing SFL or RHO are functionally separable. Distinct Golgi units containing FRC and RHO in embryos could also be separated biochemically by immunoisolation techniques. We also show that Tn-antigen glycan is localized only in a subset of the Golgi units distributed basally in a polarized cell. We propose that the different localizations among distinct Golgi units of molecules involved in glycosylation underlie the diversity of glycan modification.

Indexed as

AnimalsDrosophilaDrosophila ProteinsGlycosylationGolgi ApparatusPolysaccharidesProtein Processing, Post-TranslationalProtein TransportDrosophila ProteinsPolysaccharides

Identifiers

PMID16174741
PMCPMC1224666
OpenAlexW2002148997

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.