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Molecular machinery for non-vesicular trafficking of ceramide

Author

Listed:
  • Kentaro Hanada

    (National Institute of Infectious Diseases)

  • Keigo Kumagai

    (National Institute of Infectious Diseases)

  • Satoshi Yasuda

    (National Institute of Infectious Diseases)

  • Yukiko Miura

    (National Institute of Infectious Diseases)

  • Miyuki Kawano

    (National Institute of Infectious Diseases)

  • Masayoshi Fukasawa

    (National Institute of Infectious Diseases)

  • Masahiro Nishijima

    (National Institute of Infectious Diseases)

Abstract

Synthesis and sorting of lipids are essential for membrane biogenesis; however, the mechanisms underlying the transport of membrane lipids remain little understood. Ceramide is synthesized at the endoplasmic reticulum and translocated to the Golgi compartment for conversion to sphingomyelin. The main pathway of ceramide transport to the Golgi is genetically impaired in a mammalian mutant cell line, LY-A. Here we identify CERT as the factor defective in LY-A cells. CERT, which is identical to a splicing variant of Goodpasture antigen-binding protein, is a cytoplasmic protein with a phosphatidylinositol-4-monophosphate-binding (PtdIns4P) domain and a putative domain for catalysing lipid transfer. In vitro assays show that this lipid-transfer-catalysing domain specifically extracts ceramide from phospholipid bilayers. CERT expressed in LY-A cells has an amino acid substitution that destroys its PtdIns4P-binding activity, thereby impairing its Golgi-targeting function. We conclude that CERT mediates the intracellular trafficking of ceramide in a non-vesicular manner.

Suggested Citation

  • Kentaro Hanada & Keigo Kumagai & Satoshi Yasuda & Yukiko Miura & Miyuki Kawano & Masayoshi Fukasawa & Masahiro Nishijima, 2003. "Molecular machinery for non-vesicular trafficking of ceramide," Nature, Nature, vol. 426(6968), pages 803-809, December.
    • Handle: RePEc:nat:nature:v:426:y:2003:i:6968:d:10.1038_nature02188
    DOI: 10.1038/nature02188
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