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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Diverse polysaccharides are installed on specific asparagine residues as glycoproteins traverse the endoplasmic reticulum and Golgi. These N-glycan structures comprise the N-glycome, which coats cell surfaces, regulates cell–cell and cell–matrix interactions, and has functional consequences for immune system function and beyond. Our understanding of how intracellular signaling regulates the molecular architecture of the N-glycome remains immature. We show that the transcription factor XBP1s alters N-glycan structures displayed on endogenous membrane-associated and secreted glycoproteins, coincident with XBP1s-induced changes in N-glycosylation–related transcripts. These results establish a role for the unfolded protein response in defining the global composition of the N-glycome–providing a mechanism for transducing internal stress to an external signal, a phenomenon with implications for both normal biology and pathology.

XBP1s activation can globally remodel N-glycan structure distribution patterns