Medical Journals

Cert and Intracellular Trafficking of Ceramide.

Authors:
  • Hanada Kentaro
  • Kumagai Keigo
  • Tomishige Nario
  • Kawano Miyuki

From: Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo, 162-8640, Japan. hanak@nih.go.jp

Biochimica et biophysica acta

  • Publish Date: Jun 2007
  • ISSN: 0006-3002
  • Volume: 1771
  • Issue: 6
  • Pages: 644-53
  • Medium: Print
  • Language: English
  • Citation (JAMA): Hanada Kentaro, Kumagai Keigo, Tomishige Nario, et al. Cert and Intracellular Trafficking of Ceramide.. Biochim. Biophys. Acta Jun 2007;1771:644-53

Abstract

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, ceramide is newly produced at the endoplasmic reticulum (ER), and transported from the ER to the trans Golgi regions, where it is converted to sphingomyelin. CERT has been identified as a key factor for the ER-to-Golgi trafficking of ceramide. CERT contains several functional domains including (i) a START domain capable of catalyzing inter-membrane transfer of ceramide, (ii) a pleckstrin homology domain, which serves to target the Golgi apparatus by recognizing phosphatidylinositol 4-monophosphate, and (iii) a short peptide motif named FFAT motif which interacts with the ER-resident membrane protein VAP. CERT is preferentially distributed to the Golgi region in cells, and Golgi-targeted CERT appears to retain the activity to interact with VAP. On the basis of these results, it has been proposed that CERT extracts ceramide from the ER and carries it to the Golgi apparatus in a non-vesicular manner and that a particularly efficient cycle of CERT movement for trafficking of ceramide may proceed at membrane contact sites between the ER and the Golgi apparatus.

Mesh Headings (Keywords): Amino Acid Motifs, Amino Acid Sequence, Animals, Biological Transport, Cell Line, Ceramides, Cricetinae, Endoplasmic Reticulum, Humans, Intracellular Space, Protein-Serine-Threonine Kinases, Sphingomyelins, trans-Golgi Network


Check for Full Text / PubMed Unique Identifier (PMID): 17314061


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

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The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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