ArticleMolecular biology of the cell2013
Apical sorting of lysoGPI-anchored proteins occurs independent of association with detergent-resistant membranes but dependent on their N-glycosylation.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Posttranslational microtubule modification alters podocalyxin-trafficking in epithelial cells.Frontiers in cell and developmental biology · 2025Article
- Linking glycosphingolipid metabolism to disease-related changes in the plasma membrane proteome.Biochemical Society transactions · 2024Review
- Cell type-specific delivery by modular envelope design.Nature communications · 2023Article
- Lipid rafts and neurodegeneration: structural and functional roles in physiologic aging and neurodegenerative diseases.Journal of lipid research · 2020Review
- Trafficking and Function of the Voltage-Gated Sodium Channel β2 Subunit.Biomolecules · 2019Review
- The Rab11-binding protein RELCH/KIAA1468 controls intracellular cholesterol distribution.The Journal of cell biology · 2018Article
- Newly synthesized and recycling pools of the apical protein gp135 do not occupy the same compartments.Traffic (Copenhagen, Denmark) · 2016Article
- Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface.Journal of lipid research · 2016Review
- Biosynthesis of GPI-anchored proteins: special emphasis on GPI lipid remodeling.Journal of lipid research · 2016Review
- O-glycans direct selectin ligands to lipid rafts on leukocytes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most glycosylphosphatidylinositol-anchored proteins (GPI-APs) are located at the apical surface of epithelial cells. The apical delivery of GPI-APs is believed to result from their association with lipid rafts. We find that overexpression of C-terminally tagged PGAP3 caused predominant production of lysoGPI-APs, an intermediate precursor in the GPI lipid remodeling process in Madin-Darby canine kidney cells. In these cells, produced lysoGPI-APs are not incorporated into detergent-resistant membranes (DRMs) but still are delivered apically, suggesting that GPI-AP association with DRMs is not necessary for apical targeting. In contrast, apical transport of both fully remodeled and lyso forms of GPI-APs is dependent on N-glycosylation, confirming a general role of N-glycans in apical protein transport. We also find that depletion of cholesterol causes apical-to-basolateral retargeting not only of fully remodeled GPI-APs, but also of lysoGPI-APs, as well as endogenous soluble and transmembrane proteins that would normally be targeted to the apical membrane. These findings confirm the essential role for cholesterol in the apical protein targeting and further demonstrate that the mechanism of cholesterol-dependent apical sorting is not related to DRM association of GPI-APs.
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