Opendata, web and dolomites


Nucleocytoplasmic O-glycosylation in Yeast

Total Cost €


EC-Contrib. €






Project "Yeast-Glyco" data sheet

The following table provides information about the project.


Organization address
address: NORREGADE 10
postcode: 1165

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Denmark [DK]
 Project website
 Total cost 278˙227 €
 EC max contribution 278˙227 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2015
 Funding Scheme MSCA-IF-GF
 Starting year 2016
 Duration (year-month-day) from 2016-10-01   to  2019-09-30


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    KOBENHAVNS UNIVERSITET DK (KOBENHAVN) coordinator 278˙227.00


 Project objective

Signal transduction via post-translational modifications (PTMs) of proteins maintains essential cellular processes in all eukaryotes. Similar to protein phosphorylation, O-GlcNAcylation is a vital signaling mechanism that involves the dynamic cycling of sugar molecules on proteins and these PTMs exhibit extensive crosstalk for regulation of core cellular processes. The only eukaryotic cell type that lacks both signaling mechanisms is yeast and it has been difficult to understand how yeast survive without the essential functions of O-GlcNAcylation. This proposal is based on our discovery demonstrating that baker’s yeast has an O-linked mannose (O-Man) glycosylation system that operates in nuclear, cytoplasmic and mitochondrial compartments. The localization of these O-Man modifications on yeast proteins mirrors that of O-GlcNAcylation found in higher eukaryotes and this discovery demonstrates that yeast possess a hitherto unknown signaling mechanism involved a myriad of cellular processes. This research project aims to explore when and where yeast utilize the nucleocytoplasmic O-Man signaling system and to understand the functional consequences of this novel modification. In addition, the project aims to identify and characterize the enzymes responsible for the attachment and removal of nucleocytoplasmic O-Man modifications in order to enable manipulation of the system for improvements in yeast-based bioproduction and bioprocessing platforms. The project will open an entirely new area of research by bringing novel knowledge on how yeast orchestrate cellular signaling and advance our understanding on how essential cellular processes are controlled in eukaryotes. This holds promise to bring unique opportunities to manipulate yeast for improvements and open for wide applications in industry and biotechnology.


year authors and title journal last update
List of publications.
2019 Ida Signe Bohse Larsen, Yoshiki Narimatsu, Henrik Clausen, Hiren J Joshi, Adnan Halim
Multiple distinct O-Mannosylation pathways in eukaryotes
published pages: 171-178, ISSN: 0959-440X, DOI: 10.1016/
Current Opinion in Structural Biology 56 2020-03-20
2017 Ida Signe Bohse Larsen, Yoshiki Narimatsu, Hiren Jitendra Joshi, Zhang Yang, Oliver J. Harrison, Julia Brasch, Lawrence Shapiro, Barry Honig, Sergey Y. Vakhrushev, Henrik Clausen, Adnan Halim
Mammalian O -mannosylation of cadherins and plexins is independent of protein O -mannosyltransferases 1 and 2
published pages: 11586-11598, ISSN: 0021-9258, DOI: 10.1074/jbc.M117.794487
Journal of Biological Chemistry 292/27 2020-03-20
2017 Adnan Halim, Jan Haug Anonsen
Microbial glycoproteomics
published pages: 143-150, ISSN: 0959-440X, DOI: 10.1016/
Current Opinion in Structural Biology 44 2020-03-20
2017 Ida Signe Bohse Larsen, Yoshiki Narimatsu, Hiren Jitendra Joshi, Lina Siukstaite, Oliver J. Harrison, Julia Brasch, Kerry M. Goodman, Lars Hansen, Lawrence Shapiro, Barry Honig, Sergey Y. Vakhrushev, Henrik Clausen, Adnan Halim
Discovery of an O-mannosylation pathway selectively serving cadherins and protocadherins
published pages: 11163-11168, ISSN: 0027-8424, DOI: 10.1073/pnas.1708319114
Proceedings of the National Academy of Sciences 114/42 2020-03-20

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