Mannose trimming is the dominant signal for the release of misfolded glycoproteins from ER quality control.

ABSTRACT: N-glycosylation is essential for protein folding in the endoplasmic reticulum (ER). Glycan attachment facilitates the binding of newly synthesized polypeptides to calnexin and calreticulin, two ER-resident lectins that act as chaperones and promote folding. The regulatory mechanism underlying this process is dictated by the glycan composition, and this study has elucidated the function of mannose trimming in the release of misfolded glycoprotein from ER quality control and subsequent transfer to ER-associated degradation (ERAD) in plants. Coimmunoprecipitation experiments were performed to investigate the interaction between the ERAD substrate SUBEX-C57Y and ER-resident lectins, providing evidence for a specific interaction with calnexin. Furthermore, the results show that the expression o

SUBMITTER: Shin YJ 

PROVIDER: S-EPMC12494556 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature