University of Oulu

Khoder-Agha, F., Sosicka, P., Escriva Conde, M., Hassinen, A., Glumoff, T., Olczak, M., & Kellokumpu, S. (2019). N-acetylglucosaminyltransferases and nucleotide sugar transporters form multi-enzyme–multi-transporter assemblies in golgi membranes in vivo. Cellular and Molecular Life Sciences, 76(9), 1821–1832.

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

Saved in:
Author: Khoder-Agha, Fawzi1; Sosicka, Paulina2,3; Escriva Conde, Maria1,4;
Organizations: 1Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland
2Laboratory of Biochemistry, Faculty of Biotechnology University of Wroclaw, Wrocław, Poland
3Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, USA
4Faculty of Biology, University of Barcelona, Barcelona, Spain
5Institute of Molecular Medicine, Helsinki, Finland
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 2.2 MB)
Persistent link:
Language: English
Published: Springer Nature, 2019
Publish Date: 2019-06-05


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.

see all

Series: Cellular and molecular life sciences
ISSN: 1420-682X
ISSN-E: 1420-9071
ISSN-L: 1420-682X
Volume: 76
Issue: 9
Pages: 1821 - 1832
DOI: 10.1007/s00018-019-03032-5
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
Funding: We wish to thank the National Science Centre (NCN), Krakow, Poland for the funding (grant no. 2014/15/N/NZ1/00492). We also thank the Academy of Finland for funding to SK (grant no. 285232, 2015). PS research visit in Oulu was supported by grant no. 2016/20/T/NZ3/00534 from the National Science Centre (NCN), Krakow, Poland. The authors also greatly acknowledge prof. Pamela Stanley (New York, USA) for many helpful comments on the manuscript. Open access funding provided by University of Oulu including Oulu University Hospital.
Academy of Finland Grant Number: 285232
Detailed Information: 285232 (Academy of Finland Funding decision)
Dataset Reference: Supplementary material
Copyright information: This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.