RT Journal Article
T1 Quality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit sites.
A1 Rodriguez-Gallardo, Sofia
A1 Sabido-Bozo, Susana
A1 Ikeda, Atsuko
A1 Araki, Misako
A1 Okazaki, Kouta
A1 Nakano, Miyako
A1 Aguilera-Romero, Auxiliadora
A1 Cortes-Gomez, Alejandro
A1 Lopez, Sergio
A1 Waga, Miho
A1 Nakano, Akihiko
A1 Kurokawa, Kazuo
A1 Muñiz, Manuel
A1 Funato, Kouichi
K1 CP: Cell biology
K1 CP: Molecular biology
K1 GPI-anchored protein
K1 ceramide remodeling
K1 endoplasmic reticulum
K1 glycan remodeling
K1 protein sorting
K1 quality control
K1 yeast Saccharomyces cerevisiae
AB 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.
YR 2022
FD 2022
LK http://hdl.handle.net/10668/22076
UL http://hdl.handle.net/10668/22076
LA en
DS RISalud
RD Apr 11, 2025