Molecular machinery for non-vesicular trafficking of ceramide

@article{Hanada2003MolecularMF,
  title={Molecular machinery for non-vesicular trafficking of ceramide},
  author={Kentaro Hanada and Keigo Kumagai and Satoshi Yasuda and Yukiko Miura and Miyuki Kawano and Masayoshi Fukasawa and Masahiro Nishijima},
  journal={Nature},
  year={2003},
  volume={426},
  pages={803-809}
}
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… 
CERT-mediated trafficking of ceramide.
TLDR
CERT mediates the ER-to-Golgi trafficking of ceramide and it has been suggested that CERT extracts ceramide from the ER and carries it to the Golgi apparatus in a non-vesicular manner and that efficient CERT-mediated trafficking of Ceramide occurs at membrane contact sites between theER and the Gol Gi apparatus.
CERT and intracellular trafficking of ceramide.
The transport and sorting of lipids from the sites of their synthesis to their appropriate destinations are fundamental for membrane biogenesis. In the synthesis of sphingolipids in mammalian cells,
Molecular mechanisms and regulation of ceramide transport.
TLDR
The identification of organellar targeting motifs in other related lipid-binding/transport proteins indicate that concepts learned from the study of ceramide transport can be applied to other lipid transport processes.
Molecular Mechanism of Ceramide Trafficking from the Endoplasmic Reticulum to the Golgi Apparatus in Mammalian Cells
Synthesis and sorting of lipids are essential events for membrane biogenesis and its homeostasis. The endoplasmic reticulum (ER) is the center of the de novo synthesis of various lipid types.
Interorganelle Trafficking of Ceramide Is Regulated by Phosphorylation-dependent Cooperativity between the PH and START Domains of CERT*
TLDR
In vitro assays show that the phosphorylation induces an autoinhibitory interaction between the PH and START domains and consequently inactivates both the phosphoinositide binding and ceramide transfer activities of CERT, a novel molecular event to regulate the intracellular trafficking of ceramide.
Efficient Trafficking of Ceramide from the Endoplasmic Reticulum to the Golgi Apparatus Requires a VAMP-associated Protein-interacting FFAT Motif of CERT*
TLDR
It is suggested that the Golgi-targeting PH domain and ER-interacting FFAT motif of CERT spatially restrict the random ceramide transfer activity of the START domain in cells.
CERT Mediates Intermembrane Transfer of Various Molecular Species of Ceramides*
TLDR
Results indicate that CERT can mediate transfer of various types of ceramides that naturally exist and their close relatives and also recognizes short chain fluorescent analogs of ceramide with a stoichiometry of 1:1.
Intracellular trafficking of ceramide by ceramide transfer protein
  • K. Hanada
  • Chemistry, Medicine
    Proceedings of the Japan Academy. Series B, Physical and biological sciences
  • 2010
TLDR
The transport and sorting of lipids are fundamental to membrane biogenesis and it has been suggested that CERT extracts ceramide from the ER and carries it to the Golgi apparatus in a non-vesicular manner and that efficient CERT-mediated trafficking of ceramide occurs at membrane contact sites between theER and the Gol Gi apparatus.
Sphingomyelin organization is required for vesicle biogenesis at the Golgi complex
TLDR
C6‐sphingomyelin prevented liquid‐ordered domain formation in giant unilamellar vesicles and reduced the lipid order in the Golgi membranes of HeLa cells, highlighting the importance of a regulated production and organization of sphingomylin in the biogenesis of transport carriers at the Gol Gi membranes.
Phosphoregulation of the Ceramide Transport Protein CERT at Serine 315 in the Interaction with VAMP-associated Protein (VAP) for Inter-organelle Trafficking of Ceramide in Mammalian Cells*
TLDR
It is demonstrated that the phosphorylation of CERT at the FFAT motif-adjacent serine affected its affinity for VAP, which may regulate the inter-organelle trafficking of ceramide in response to the perturbation of cellular sphingomyelin and/or other sphingolipids.
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