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Cited by 1,209Lipid Membrane Structure and BehaviorCaveolin-1 and cellular processesCellular transport and secretion

GPI-anchored proteins are organized in submicron domains at the cell surface

Varma, Rajat, Mayor, Satyajit·1998·Nature
DOI 10.1038/29563
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Abstract

Lateral heterogeneities in the classical fluid-mosaic model of cell membranes are now envisaged as domains or 'rafts' that are enriched in (glyco)sphingolipids, cholesterol, specific membrane proteins and glycosylphosphatidylinositol (GPI)-anchored proteins. These rafts dictate the sorting of associated proteins and/or provide sites for assembling cytoplasmic signalling molecules. However, there is no direct evidence that rafts exist in living cells. We have now measured the extent of energy transfer between isoforms of the folate receptor bound to a fluorescent analogue of folic acid, in terms of the dependence of fluorescence polarization on fluorophore densities in membranes. We find that the extent of energy transfer for the GPI-anchored folate-receptor isoform is density-independent, which is characteristic of organization in sub-pixel-sized domains at the surface of living cells; however, the extent of energy transfer for the transmembrane-anchored folate-receptor isoform was density-dependent, which is consistent with a random distribution. These domains are likely to be less than 70 nm in diameter and are disrupted by removal of cellular cholesterol. These results indicate that lipid-linked proteins are organized in cholesterol-dependent submicron-sized domains. Our methodology offers a new way of monitoring nanometre-scale association between molecules in living cells.

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Crossref · 10.1038/29563

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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 [539]

  • 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 [539]

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Authors
Varma, R., & Mayor, S.
Affiliations
National Centre for Biological Sciences (IN)
Corresponding author
Mayor, Satyajit
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1998-08
Volume
394
Issue
6695
Pages
798-801
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/29563
OpenAlex
W1635401440
Cited by
1,209
References
31
Citations by year
2026: 11 · 2025: 8 · 2024: 15 · 2023: 20 · 2022: 14 · 2021: 17 · 2020: 24 · 2019: 24 · 2018: 23 · 2017: 27 · 2016: 23 · 2015: 41 · 2014: 37 · 2013: 27 · 2012: 45
FWCI
30.12
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
GPI-anchored proteins, lipid rafts, folate receptor, energy transfer, fluorescence polarization, cholesterol, membrane heterogeneity, transmembrane proteins
MeSH terms
Animals, Carrier Proteins, Cell Membrane, Cholesterol, Energy Transfer, Fluoresceins, Fluorescence Polarization, Folic Acid, Cricetinae, Lysine, Receptors, Cell Surface, Transfection, CHO Cells, Glycosylphosphatidylinositols, Folate Receptors, GPI-Anchored

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