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

In the endoplasmic reticulum (ER), N-linked glycans (N-glycans) function as signals to recruit the lectin chaperones involved in protein folding, quality control and ER-associated degradation. We undertook a systematic study of the four N-glycans of mutated carboxypeptidase yscY (CPY*) to determine whether there are positional differences between the glycans in ER-associated degradation. We constructed hypoglycosylated CPY* variants containing one, two or three N-glycans in various combinations and studied their degradation kinetics. We found that the four carbohydrate chains on CPY* are not equal in their signaling function: presence of the Asn368-linked glycan is necessary and sufficient for efficient degradation of CPY*. We also analysed the involvement of the ER lectins Htm1p and Cne1p (yeast calnexin) in the glycan-based recognition process with respect to number and position of N-glycans. We observed that Htm1p function depends on the presence of N-glycans in general but that there is no positional preference for a particular glycan. Cne1p, however, is selective with respect to substrate, and participates in the quality control only of some underglycosylated variants. For cases in which both lectins are involved, Cne1p and Htm1p play competing roles in targeting the substrate for degradation: loss of Cne1p accelerates degradation, whereas loss of Htm1p stabilizes the substrate.

Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation