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• W2077237389 abstract "Glycosylphosphatidylinositol (GPI) anchoring of proteins is a posttranslational modification occurring in the endoplasmic reticulum (ER). After GPI attachment, proteins are transported by coat protein complex II (COPII)-coated vesicles from the ER. Because GPI-anchored proteins (GPI-APs) are localized in the lumen, they cannot interact with cytosolic COPII components directly. Receptors that link GPI-APs to COPII are thought to be involved in efficient packaging of GPI-APs into vesicles; however, mechanisms of GPI-AP sorting are not well understood. Here we describe two remodeling reactions for GPI anchors, mediated by PGAP1 and PGAP5, which were required for sorting of GPI-APs to ER exit sites. The p24 family of proteins recognized the remodeled GPI-APs and sorted them into COPII vesicles. Association of p24 proteins with GPI-APs was pH dependent, which suggests that they bind in the ER and dissociate in post-ER acidic compartments. Our results indicate that p24 complexes act as cargo receptors for correctly remodeled GPI-APs to be sorted into COPII vesicles." @default.
• W2077237389 created "2016-06-24" @default.
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• W2077237389 date "2011-07-04" @default.
• W2077237389 modified "2023-09-24" @default.
• W2077237389 title "Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI" @default.
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• W2077237389 doi "https://doi.org/10.1083/jcb.201012074" @default.
• W2077237389 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3135397" @default.
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• W2077237389 hasPublicationYear "2011" @default.
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