Explore the words cloud of the Yeast-Glyco project. It provides you a very rough idea of what is the project "Yeast-Glyco" about.
The following table provides information about the project.
|Coordinator Country||Denmark [DK]|
|Total cost||278˙227 €|
|EC max contribution||278˙227 € (100%)|
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
|Duration (year-month-day)||from 2016-10-01 to 2019-09-30|
Take a look of project's partnership.
|1||KOBENHAVNS UNIVERSITET||DK (KOBENHAVN)||coordinator||278˙227.00|
|2||THE ROCKEFELLER UNIVERSITY NOT FOR PROFIT CORPORATION||US (NEW YORK)||partner||0.00|
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|
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/j.sbi.2019.03.003
|Current Opinion in Structural Biology 56||2020-03-20|
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|
Adnan Halim, Jan Haug Anonsen
published pages: 143-150, ISSN: 0959-440X, DOI: 10.1016/j.sbi.2017.03.005
|Current Opinion in Structural Biology 44||2020-03-20|
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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