Evidence map›Paper›PMID 25246532›Full record

ArticleThe Journal of biological chemistry2014

Golgi phosphoprotein 3 triggers signal-mediated incorporation of glycosyltransferases into coatomer-coated (COPI) vesicles.

Elias S P Eckert, Ingeborg Reckmann, Andrea Hellwig, Simone Röhling, Assou El-Battari, Felix T Wieland, Vincent Popoff

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
1.8field-weighted citation impact, top 17% 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

48 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Article
  3. Mining cancer genomes for copy number alterations identifies glycosylation enzymes as oncogenic drivers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Role of theFrontiers in cell and developmental biology · 2022
    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

7 authors at 2 institutions in 2 countries.

Elias S P EckertFrom the Heidelberg University Biochemistry Center (BZH), INF 328 and.
Ingeborg ReckmannFrom the Heidelberg University Biochemistry Center (BZH), INF 328 and.
Andrea HellwigInterdisciplinary Center for Neurosciences (IZN), INF 364, Heidelberg University, 69120 Heidelberg, Germany and.
Simone RöhlingFrom the Heidelberg University Biochemistry Center (BZH), INF 328 and.
Assou El-BattariINSERM UMR 911, Aix-Marseille Université, Centre de Recherche en Oncobiologie et Oncopharmacologie (CR02), 13284 Marseille, France.
Felix T WielandFrom the Heidelberg University Biochemistry Center (BZH), INF 328 and.
Vincent PopoffFrom the Heidelberg University Biochemistry Center (BZH), INF 328 and vincent.popoff@espci.org.
Heidelberg University · DEAix-Marseille Université · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Newly synthesized membrane and secreted proteins undergo a series of posttranslational modifications in the Golgi apparatus, including attachment of carbohydrate moieties. The final structure of so-formed glycans is determined by the order of execution of the different glycosylation steps, which seems intimately related to the spatial distribution of glycosyltransferases and glycosyl hydrolases within the Golgi apparatus. How cells achieve an accurate localization of these enzymes is not completely understood but might involve dynamic processes such as coatomer-coated (COPI) vesicle-mediated trafficking. In yeast, this transport is likely to be regulated by vacuolar protein sorting 74 (Vps74p), a peripheral Golgi protein able to interact with COPI coat as well as with a binding motif present in the cytosolic tails of some mannosyltransferases. Recently, Golgi phosphoprotein 3 (GOLPH3), the mammalian homolog of Vps74, has been shown to control the Golgi localization of core 2 N-acetylglucosamine-transferase 1. Here, we highlight a role of GOLPH3 in the spatial localization of α-2,6-sialyltransferase 1. We show, for the first time, that GOLPH3 supports incorporation of both core 2 N-acetylglucosamine-transferase 1 and α-2,6-sialyltransferase 1 into COPI vesicles. Depletion of GOLPH3 altered the subcellular localization of these enzymes. In contrast, galactosyltransferase, an enzyme that does not interact with GOLPH3, was neither incorporated into COPI vesicles nor was dependent on GOLPH3 for proper localization.

Indexed as

Gene Expression RegulationAnimalsAntigens, CDbeta-D-Galactoside alpha 2-6-SialyltransferaseCarrier ProteinsCHO CellsCoatomer ProteinCOP-Coated VesiclesCricetinaeCricetulusCytosolGalactosyltransferasesGlycosyltransferasesGolgi ApparatusHumansMembrane ProteinsAntigens, CDbeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-acetylglucosaminyl transferasebeta-D-Galactoside alpha 2-6-SialyltransferaseCarrier ProteinsCoatomer ProteinGalactosyltransferasesGlycosyltransferasesGOLPH3 protein, humanMembrane ProteinsN-AcetylglucosaminyltransferasesRecombinant ProteinsSialyltransferasesST6GAL1 protein, humanCOPIGlycosyltransferasesGolgiSialyltransferaseTraffickingVesicles

Identifiers

PMID25246532
PMCPMC4223332
OpenAlexW2043462612

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.