Scientific article
OA Policy
English

Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast

Published inThe Journal of biological chemistry, vol. 277, no. 51, p. 49538-49544
Publication date2002-12-20
Abstract

Ongoing sphingolipid synthesis is specifically required in vivo for the endoplasmic reticulum (ER) to Golgi transport of glycosylphosphatidylinositol (GPI)-anchored proteins. However, the sphingolipid intermediates that are required for transport nor their role(s) have been indentified. Using stereoisomers of dihydrosphingosine, together with specific inhibitors and a mutant defective for sphingolipid synthesis, we now show that ceramides and/or inositol sphingolipids are indispensable for GPI-anchored protein transport. Furthermore, in the absence of sphingolipid synthesis, a significant fraction of GPI-anchored proteins is no longer associated tightly with the ER membrane. The loose membrane association is neither because of the lack of a GPI-anchor nor because of prolonged ER retention of GPI-anchored proteins. These results indicate that ceramides and/or inositol sphingolipids are required to stabilize the association of GPI-anchored proteins with membranes. They could act either by direct involvement as membrane components or as substrates for the remodeling of GPI liquid moieties.

Citation (ISO format)
WATANABE CASTILLON, Reika et al. Sphingolipids are required for the stable membrane association of glycosylphosphatidylinositol-anchored proteins in yeast. In: The Journal of biological chemistry, 2002, vol. 277, n° 51, p. 49538–49544. doi: 10.1074/jbc.M206209200
Main files (1)
Article (Published version)
accessLevelPublic
Identifiers
Journal ISSN0021-9258
141views
60downloads

Technical informations

Creation25/01/2023 14:58:00
First validation25/01/2023 14:58:00
Update time16/03/2023 10:30:29
Status update16/03/2023 10:30:29
Last indexation01/11/2024 04:01:46
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack