English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

Significance Nucleocytoplasmic dynamic cycling ofN -Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) and phosphorylation coregulate important cellular processes in all eukaryotic organisms except yeast, includingSaccharomyces cerevisiae andSchizosaccharomyces pombe . The lack of an equivalent nucleocytoplasmic O-glycosylation system in yeast has been difficult to explain given that O-GlcNAcylation is an essential modification in higher organisms. Here, we reveal that yeast use O-linked mannose to modify nucleocytoplasmic proteins on evolutionary-conserved regions and sites normally occupied by O-GlcNAc in higher eukaryotes. The results presented in this study open new avenues for exploration of nutrient sensing and signaling events based on nucleocytoplasmic O-glycosylation in yeast.

Discovery of a nucleocytoplasmic O-mannose glycoproteome in yeast