Evidence map›Paper›PMID 24733390›Full record

ArticleThe Journal of biological chemistry2014

Golgi phosphoprotein 3 mediates the Golgi localization and function of protein O-linked mannose β-1,2-N-acetlyglucosaminyltransferase 1.

Natasha A Pereira, Helen X Pu, Hazel Goh, Zhiwei Song

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 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Golgi Drivers of Cancer.Sub-cellular biochemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. GOLPH3 keeps the Golgi residents at home.The Journal of cell biology · 2021
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  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 at 1 institution in 1 country.

Natasha A PereiraFrom the Bioprocessing Technology Institute, Agency for Science, Technology, and Research (A*STAR), 20 Biopolis Way, 06-01 Centros, 138668, Singapore.
Helen X PuFrom the Bioprocessing Technology Institute, Agency for Science, Technology, and Research (A*STAR), 20 Biopolis Way, 06-01 Centros, 138668, Singapore.
Hazel GohFrom the Bioprocessing Technology Institute, Agency for Science, Technology, and Research (A*STAR), 20 Biopolis Way, 06-01 Centros, 138668, Singapore.
Zhiwei SongFrom the Bioprocessing Technology Institute, Agency for Science, Technology, and Research (A*STAR), 20 Biopolis Way, 06-01 Centros, 138668, Singapore song_zhiwei@bti.a-star.edu.sg.
Agency for Science, Technology and Research · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GOLPH3 is a highly conserved protein found across the eukaryotic lineage. The yeast homolog, Vps74p, interacts with and maintains the Golgi localization of several mannosyltransferases, which is subsequently critical for N- and O-glycosylation in yeast. Through the use of a T7 phage display, we discovered a novel interaction between GOLPH3 and a mammalian glycosyltransferase, POMGnT1, which is involved in the O-mannosylation of α-dystroglycan. The cytoplasmic tail of POMGnT1 was found to be critical for mediating its interaction with GOLPH3. Loss of this interaction resulted in the inability of POMGnT1 to localize to the Golgi and reduced the functional glycosylation of α-dystroglycan. In addition, we showed that three clinically relevant mutations present in the stem domain of POMGnT1 mislocalized to the endoplasmic reticulum, highlighting the importance of identifying the molecular mechanisms responsible for Golgi localization of glycosyltransferases. Our findings reveal a novel role for GOLPH3 in mediating the Golgi localization of POMGnT1.

Indexed as

Blotting, WesternDystroglycansEndoplasmic ReticulumGene ExpressionGlycosylationGolgi ApparatusHEK293 CellsHeLa CellsHumansMembrane ProteinsMicroscopy, FluorescenceMutationN-AcetylglucosaminyltransferasesProtein BindingReverse Transcriptase Polymerase Chain ReactionRNA InterferenceDystroglycansGOLPH3 protein, humanMembrane ProteinsN-Acetylglucosaminyltransferasesprotein O-mannose beta-1,2-N-acetylglucosaminyltransferaseGlycosylationGlycosyltransferasesGOLPH3Muscle-eye Brain DiseasePOMGnTProtein-protein InteractionsProtein TargetingSkeletal Muscle

Identifiers

PMID24733390
PMCPMC4031531
OpenAlexW1988337854

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.