Abstract
In mammalian cells, ceramides are central lipids in sphingolipid metabolism and serve both as signaling lipids and as precursors for other bioactive sphingolipids, ranging from complex glycosphingolipids to “simpler” lipids such as ceramide-1-phosphate, sphingomyelin (SM), sphingosine and sphingosine-1-phosphate (S1P).
Highlights
In mammalian cells, ceramides are central lipids in sphingolipid metabolism and serve both as signaling lipids and as precursors for other bioactive sphingolipids, ranging from complex glycosphingolipids to “simpler” lipids such as ceramide-1-phosphate, sphingomyelin (SM), sphingosine and sphingosine-1-phosphate (S1P)
FFAT domain can be phosphorylated on its serine 315 (S315), which improves ceramide transport from endoplasmic reticulum (ER) to Golgi, since CERT displays a higher affinity to VAMP-associated protein (VAP) when S315 is phosphorylated (Figure 2) [7]
All these results suggest again that CERT expression remains crucial in order to prevent ceramides to harm the cells
Summary
Ceramides are central lipids in sphingolipid metabolism and serve both as signaling lipids and as precursors for other bioactive sphingolipids, ranging from complex glycosphingolipids to “simpler” lipids such as ceramide-1-phosphate, sphingomyelin (SM), sphingosine and sphingosine-1-phosphate (S1P). Ceramides consist of a spingoid long chain base to which a fatty acid is attached via an amide bond They can be generated either by hydrolysis of sphingomyelin by sphingomyelinases, degradation of complex sphingolipids localized in lysosomes, or produced de novo from saturated fatty acids, like palmitic acid, in the endoplasmic reticulum (ER) [2]. Synthesis of both SM and glucosylceramides (GlcCer) from ceramide occurs into the Golgi apparatus [2]. Two phenylalanine residues localized in the acidic tract (FFAT) domain allows CERT to bind the VAMP-associated protein (VAP) in the ER membrane [7].
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