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

Calnexin is a chaperone protein that plays a critical role in glycoprotein folding in the endoplasmic reticulum (ER). The function of calnexin depends on its binding to monoglucosylated oligosaccharides on nascent glycoproteins, whereas the generation of monoglucosylated oligosaccharides depends on the activity of α-glucosidases I and II, which trim off terminal glucose residues sequentially from triglucosylated N-glycans. This biochemical mechanism can be exploited to study calnexin-assisted folding and subsequent ER exiting of glycoproteins in cells. In our investigation of the intracellular trafficking of N-glycosylated serine proteases, we used an inhibitor of α-glucosidases I and II to block the trimming of triglucosylated oligosaccharides, thereby inhibiting calnexin-assisted glycoprotein folding. The study helped us to discover a key role of calnexin in the folding, ER exiting, and extracellular expression of N-glycosylated serine proteases such as corin, enteropeptidase, and prothrombin. A similar approach of glucosidase inhibition can be used to study the calnexin/calreticulin-dependent folding and intracellular trafficking of other N-glycosylated proteins.

Glucosidase Inhibition to Study Calnexin-assisted Glycoprotein Folding in Cells