Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Open accessAbstract
We show that a protein with a glycosylphosphatidyl inositol (GPI) anchor can be recovered from lysates of epithelial cells in a low density, detergent-insoluble form. Under these conditions, the protein is associated with detergent-resistant sheets and vesicles that contain other GPI-anchored proteins and are enriched in glycosphingolipids, but do not contain a basolateral marker protein. The protein is recovered in this complex only after it has been transported to the Golgi complex, suggesting that protein-sphingolipid microdomains form in the Golgi apparatus and plasma membrane and supporting the model proposed by Simons and colleagues for sorting of certain membrane proteins to the apical surface after intracellular association with glycosphingolipids.
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GPI-anchored proteins are mainly associated with glycolipid-enriched membrane microdomains and are organized in submicron domains at the cell surface.
“For example, GPI-anchored proteins are mainly associated with glycolipid-enriched membrane microdomains (538) and are organized in submicron domains at the cell surface (539).”
From Biological roles of glycans (2017) · cites this paper as [538]
Glycans can have profound effects on the organization of cell membranes.
“Glycans can have profound effects on the organization of cell membranes.”
From Biological roles of glycans (2017) · cites this paper as [538]
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“For example, GPI-anchored proteins are mainly associated with glycolipid-enriched membrane microdomains (538) and are organized in submicron domains at the cell surface (539).”
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“This is the case of GPI-anchored proteins mainly associated with glycolipid-enriched membrane microdomains interacting with lectins [39,40] or in the case of sialylated ganglioside GM3, which interacts with tyrosine kinase signaling of EGFR and insulin receptors [41–43].”
Background
- Authors
- Brown, D. A., & Rose, J. K.
- Affiliations
- Yale University (US)
- ORCID
- Brown, Deborah A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1992-02
- Volume
- 68
- Issue
- 3
- Pages
- 533-544
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2133388060
- Cited by
- 2,921
- References
- 54
- Citations by year
- 2026: 13 · 2025: 20 · 2024: 18 · 2023: 28 · 2022: 28 · 2021: 30 · 2020: 58 · 2019: 36 · 2018: 52 · 2017: 51 · 2016: 50 · 2015: 69 · 2014: 63 · 2013: 59 · 2012: 100
- FWCI
- 25.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- U.S. Public Health Service (A124345)
- National Cancer Institute (P01CA046128, CA46128)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
- Keywords
- GPI-anchored proteins, glycosphingolipids, lipid rafts, Golgi apparatus, epithelial cells, detergent-resistant membranes, basolateral sorting, protein sorting, plasma membrane
- MeSH terms
- Acid Phosphatase, Animals, Cell Compartmentation, Cell Line, Cell Membrane, Dogs, Glycolipids, Golgi Apparatus, Liposomes, Membrane Lipids, Membrane Proteins, Phosphatidylinositols, Glycosylphosphatidylinositols
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