%0 Journal Article
%A Rodriguez-Gallardo, Sofia
%A Sabido-Bozo, Susana
%A Ikeda, Atsuko
%A Araki, Misako
%A Okazaki, Kouta
%A Nakano, Miyako
%A Aguilera-Romero, Auxiliadora
%A Cortes-Gomez, Alejandro
%A Lopez, Sergio
%A Waga, Miho
%A Nakano, Akihiko
%A Kurokawa, Kazuo
%A Muñiz, Manuel
%A Funato, Kouichi
%T Quality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit sites.
%D 2022
%U http://hdl.handle.net/10668/22076
%X 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.
%K CP: Cell biology
%K CP: Molecular biology
%K GPI-anchored protein
%K ceramide remodeling
%K endoplasmic reticulum
%K glycan remodeling
%K protein sorting
%K quality control
%K yeast Saccharomyces cerevisiae
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