glycosylphosphatidylinositol; ceramide; Membranes; lipid biosynthesis; Glycosylphosphatidylinositol anchored proteins; lipid remodeling; sphingolipid; acyltransferases
Bochud A Ramachandra N Conzelmann A. (2013), Adaptation of low-resolution methods for the study of yeast microsomal polytopic membrane proteins: a methodological review., in Biochem Soc Trans.
, 41(1), 35-42.
Ramachandra N Conzelmann A. (2013), Membrane topology of yeast alkaline ceramidase YPC1, in Biochem J.
, 452(3), 585-594.
Voynova NS Vionnet C Ejsing CS Conzelmann A. (2012), A novel pathway of ceramide metabolism in Saccharomyces cerevisiae., in Biochem J.
, 447(1), 103-114.
Conzelmann A. (2012), Role of mature sphingolipids in yeast: new tools., in Mol Microbiol.
, 84(6), 991-994.
Pagac M Vazquez HM Bochud A Roubaty C Knöpfli C Vionnet C Conzelmann A. (2012), Topology of the microsomal glycerol-3-phosphate acyltransferase Gpt2p/Gat1p of Saccharomyces cerevisiae., in Mol Microbiol.
, 86(5), 1156-1166.
Pagac Martin, de la Mora Hector Vazquez, Duperrex Cécile, Roubaty Carole, Vionnet Christine, Conzelmann Andreas (2011), Topology of 1-acyl-sn-glycerol-3-phosphate acyltransferases SLC1 and ALE1 and related membrane-bound O-acyltransferases (MBOATs) of Saccharomyces cerevisiae., in The Journal of biological chemistry
, 286(42), 36438-47.
Vionnet Christine, Roubaty Carole, Ejsing Christer S, Knudsen Jens, Conzelmann Andreas (2011), Yeast cells lacking all known ceramide synthases continue to make complex sphingolipids and to incorporate ceramides into glycosylphosphatidylinositol (GPI) anchors., in The Journal of biological chemistry
, 286(8), 6769-79.
The research plan aims at a better understanding of the lipid remodeling in glycosylphosphatidylinositol (GPI) anchored proteins and its consequences for the transport and targeting of GPI proteins. We use in microsomal in vitro tests in order to understand the topology and the precise mechanisms used by the enzymes incorporating C26 fatty acids or ceramides into GPI anchors, to measure the specificity of these enzymes for their substrates and to understand how their substrates get access to the ER lumen, where lipid remodeling occurs. Since GPI proteins are partitioning into ceramide-enriched membrane domains for stability and transport, we also investigate the consequences of changes in ceramide biosynthesis for the targeting of GPI and other proteins.