Quality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit sites
Glycosylphosphatidylinositol-anchored proteins (GPI-APs) exit the endoplasmic reticulum (ER) through a specialized export pathway in the yeast Saccharomyces cerevisiae. We have recently shown that a very-long acyl chain (C26) ceramide present in the ER membrane drives clustering and sorting of GPI-A...
| Authors: | , , , , , , , , , , , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2022 |
| Country: | España |
| Institution: | Universidad de Sevilla (US) |
| Repository: | idUS. Depósito de Investigación de la Universidad de Sevilla |
| OAI Identifier: | oai:idus.us.es:11441/133541 |
| Online Access: | https://hdl.handle.net/11441/133541 https://doi.org/10.1016/j.celrep.2022.110768 |
| Access Level: | Open access |
| Keyword: | Ceramide remodeling CP: Cell biology CP: Molecular biology Endoplasmic reticulum Glycan remodeling GPI-anchored protein Protein sorting Quality control Yeast Saccharomyces cerevisiae |
| Summary: | Glycosylphosphatidylinositol-anchored proteins (GPI-APs) exit the endoplasmic reticulum (ER) through a specialized export pathway in the yeast Saccharomyces cerevisiae. We have recently shown that a very-long acyl chain (C26) ceramide present in the ER membrane drives clustering and sorting of GPI-APs into selective ER exit sites (ERES). Now, we show that this lipid-based ER sorting also involves the C26 ceramide as a lipid moiety of GPI-APs, which is incorporated into the GPI anchor through a lipid-remodeling process after protein attachment in the ER. Moreover, we also show that a GPI-AP with a C26 ceramide moiety is monitored by the GPI-glycan remodelase Ted1, which, in turn, is required for receptor-mediated export of GPI-APs. Therefore, our study reveals a quality-control system that ensures lipid-based sorting of GPI-APs into selective ERESs for differential ER export, highlighting the physiological need for this specific export pathway. |
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