Cited by 293Lipid Membrane Structure and BehaviorSphingolipid Metabolism and SignalingCaveolin-1 and cellular processes

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Assembly of Myelin by Association of Proteolipid Protein with Cholesterol- and Galactosylceramide-Rich Membrane Domains

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Simons, Mikael, Krämer, Eva-Maria, Thiele, Christoph, Stoffel, Wilhelm, Trotter, Jacqueline·2000·The Journal of Cell Biology

DOI 10.1083/jcb.151.1.143PMC PMC2189802

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Abstract

Myelin is a specialized membrane enriched in glycosphingolipids and cholesterol that contains a limited spectrum of proteins. We investigated the assembly of myelin components by oligodendrocytes and analyzed the role of lipid–protein interactions in this process. Proteolipid protein (PLP), the major myelin protein, was recovered from cultured oligodendrocytes from a low-density CHAPS-insoluble membrane fraction (CIMF) enriched in myelin lipids. PLP associated with the CIMF after leaving the endoplasmic reticulum but before exiting the Golgi apparatus, suggesting that myelin lipid and protein components assemble in the Golgi complex. The specific association of PLP with myelin lipids in CIMF was supported by the finding that it was efficiently cross-linked to photoactivable cholesterol, but not to phosphatidylcholine, which is underrepresented in both myelin and CIMF. Furthermore, depletion of cholesterol or inhibition of sphingolipid synthesis in oligodendrocytes abolished the association of PLP with CIMF. Thus, PLP may be recruited to myelin rafts, represented by CIMF, via lipid–protein interactions. In contrast to oligodendrocytes, after transfection in BHK cells, PLP is absent from isolated CIMF, suggesting that PLP requires specific lipids for raft association. In mice deficient in the enzyme ceramide galactosyl transferase, which cannot synthesize the main myelin glycosphingolipids, a large fraction of PLP no longer associates with rafts. Formation of a cholesterol- and galactosylceramide-rich membrane domain (myelin rafts) may be critical for the sorting of PLP and assembly of myelin in oligodendrocytes.

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Authors: Simons, M., Krämer, E.-M., Thiele, C., Stoffel, W., & Trotter, J.
Affiliations: Heidelberg University (DE)
aDepartment of Neurobiology, University of Heidelberg, 69120 Heidelberg, Germany
University of Cologne (DE)
ORCID: Simons, Mikael
Thiele, Christoph
Trotter, Jacqueline
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2000-10-02
Volume: 151
Issue: 1
Pages: 143-154
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.151.1.143
PMC: PMC2189802
OpenAlex: W2098744846
Cited by: 293
References: 58
Citations by year: 2026: 5 · 2025: 2 · 2024: 7 · 2023: 6 · 2022: 12 · 2021: 5 · 2020: 10 · 2019: 15 · 2018: 3 · 2017: 12 · 2016: 4 · 2015: 8 · 2014: 17 · 2013: 9 · 2012: 14
FWCI: 5.31
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
Keywords: proteolipid protein, lipid rafts, oligodendrocytes, cholesterol, galactosylceramide, glycosphingolipids, protein-lipid interactions, Golgi apparatus, sphingolipid biosynthesis
MeSH terms: Animals, Brain Chemistry, Cell Fractionation, Cholesterol, Cholic Acids, Detergents, Endoplasmic Reticulum, Galactosylceramides, Galactosyltransferases, Golgi Apparatus, Cricetinae, Myelin Sheath, Oligodendroglia, Solubility, Glycosylphosphatidylinositols, Mice, Knockout, Myelin Proteolipid Protein, Hemagglutinin Glycoproteins, Influenza Virus, Membrane Microdomains, N-Acylsphingosine Galactosyltransferase, Mice

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Assembly of Myelin by Association of Proteolipid Protein with Cholesterol- and Galactosylceramide-Rich Membrane Domains

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