Evidence map›Paper›PMID 20378551›Full record

ArticleThe Journal of biological chemistry2010

Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme complexes in live cells.

Antti Hassinen, Antti Rivinoja, Annika Kauppila, Sakari Kellokumpu

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
–field-weighted citation impact
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

48 citing papers in PubMed.

  1. Article
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  5. International journal of molecular sciences · 2023
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  6. Review
  7. Article
  8. Review
  9. Article
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  11. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. HumanProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. Review
  18. Article
  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

4 authors.

Antti HassinenDepartment of Biochemistry, University of Oulu and the Glycoscience Graduate School Finland, PO Box 3000, Linnanmaa, FIN-90014 Oulu, Finland.
Antti Rivinoja
Annika Kauppila
Sakari Kellokumpu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycans (i.e. oligosaccharide chains attached to cellular proteins and lipids) are crucial for nearly all aspects of life, including the development of multicellular organisms. They come in multiple forms, and much of this diversity between molecules, cells, and tissues is generated by Golgi-resident glycosidases and glycosyltransferases. However, their exact mode of functioning in glycan processing is currently unclear. Here we investigate the supramolecular organization of the N-glycosylation pathway in live cells by utilizing the bimolecular fluorescence complementation approach. We show that all four N-glycosylation enzymes tested (beta-1,2-N-acetylglucosaminyltransferase I, beta-1,2-N-acetylglucosaminyltransferase II, 1,4-galactosyltransferase I, and alpha-2,6-sialyltransferase I) form Golgi-localized homodimers. Intriguingly, the same enzymes also formed two distinct and functionally relevant heterodimers between the medial Golgi enzymes beta-1,2-N-acetylglucosaminyltransferase I and beta-1,2-N-acetylglucosaminyltransferase II and the trans-Golgi enzymes 1,4-galactosyltransferase I and alpha-2,6-sialyltransferase I. Given their strict Golgi localization and sequential order of function, the two heterodimeric complexes are probably responsible for the processing and maturation of N-glycans in live cells.

Indexed as

AnimalsBacterial ProteinsBase SequenceCell MembraneChlorocebus aethiopsCOS CellsDimerizationGlucosyltransferasesGlycosylationGlycosyltransferasesGolgi ApparatusHeLa CellsHumansLipidsMolecular Sequence DataPolysaccharidesBacterial ProteinsGlucosyltransferasesGlycosyltransferasesLipidsN-glycosyltransferase, Nocardia aerocolonigenesPolysaccharides

Identifiers

PMID20378551
PMCPMC2878541

What OpenQuestion holds

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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.