Molecular machinery for non-vesicular trafficking of ceramide

Kentaro Hanada (), Keigo Kumagai, Satoshi Yasuda, Yukiko Miura, Miyuki Kawano, Masayoshi Fukasawa and Masahiro Nishijima
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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

Nature, 2003, vol. 426, issue 6968, 803-809

Abstract: 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.

Date: 2003
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DOI: 10.1038/nature02188

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