Evidence map›Paper›PMID 30737517›Full record

ArticleCellular and molecular life sciences : CMLS2019

N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme-multi-transporter assemblies in golgi membranes in vivo.

Fawzi Khoder-Agha, Paulina Sosicka, Maria Escriva Conde, Antti Hassinen, Tuomo Glumoff, Mariusz Olczak, Sakari Kellokumpu

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  15. Review
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  17. Computational Modeling ofMolecules (Basel, Switzerland) · 2022
    Article
  18. Review
  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

7 authors at 4 institutions in 4 countries.

Fawzi Khoder-AghaFaculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, 90220, Oulu, Finland.
Paulina SosickaLaboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland.
Maria Escriva CondeFaculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, 90220, Oulu, Finland.
Antti HassinenFaculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, 90220, Oulu, Finland.
Tuomo GlumoffFaculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, 90220, Oulu, Finland.
Mariusz OlczakLaboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland.
Sakari KellokumpuFaculty of Biochemistry and Molecular Medicine, University of Oulu, Aapistie 7A, 90220, Oulu, Finland. sakari.kellokumpu@oulu.fi.
University of Oulu · FIDiscovery Institute · USInstitute for Molecular Medicine Finland · FIUniversity of Wrocław · PL

Funding

Academy of Finland 2015Academy of Finland 285232National Science centre 2016/20/T/NZ3/00534National Science Centre (NCN), Krakow, Poland 2014/15/N/NZ1/00492
6 · The paper itself

Abstract

Branching and processing of N-glycans in the medial-Golgi rely both on the transport of the donor UDP-N-acetylglucosamine (UDP-GlcNAc) to the Golgi lumen by the SLC35A3 nucleotide sugar transporter (NST) as well as on the addition of the GlcNAc residue to terminal mannoses in nascent N-glycans by several linkage-specific N-acetyl-glucosaminyltransferases (MGAT1-MGAT5). Previous data indicate that the MGATs and NSTs both form higher order assemblies in the Golgi membranes. Here, we investigate their specific and mutual interactions using high-throughput FRET- and BiFC-based interaction screens. We show that MGAT1, MGAT2, MGAT3, MGAT4B (but not MGAT5) and Golgi alpha-mannosidase IIX (MAN2A2) form several distinct molecular assemblies with each other and that the MAN2A2 acts as a central hub for the interactions. Similar assemblies were also detected between the NSTs SLC35A2, SLC35A3, and SLC35A4. Using in vivo BiFC-based FRET interaction screens, we also identified novel ternary complexes between the MGATs themselves or between the MGATs and the NSTs. These findings suggest that the MGATs and the NSTs self-assemble into multi-enzyme/multi-transporter complexes in the Golgi membranes in vivo to facilitate efficient synthesis of complex N-glycans.

Indexed as

alpha-MannosidaseAnimalsCell LineChlorocebus aethiopsCOS CellsGolgi ApparatusMonosaccharide Transport ProteinsMultienzyme ComplexesN-AcetylglucosaminyltransferasesNucleotide Transport ProteinsPolysaccharidesUridine Diphosphate N-Acetylglucosaminealpha-MannosidaseMonosaccharide Transport ProteinsMultienzyme ComplexesN-AcetylglucosaminyltransferasesNucleotide Transport ProteinsPolysaccharidesUridine Diphosphate N-AcetylglucosamineEnzyme complexesGlycosylationGolgi apparatusMembrane organization

Identifiers

PMID30737517
PMCPMC6453868
OpenAlexW2913843862

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.