Inositol phosphorylceramide synthase catalytic subunit AUR1 (AUR1)

The Inositol phosphorylceramide synthase catalytic subunit AUR1 (AUR1) is an enzyme in the yeast Saccharomyces cerevisiae that catalyzes the transfer of phosphorylinositol from phosphatidylinositol to ceramide, producing inositol phosphorylceramide (IPC), a key sphingolipid in fungal cell membranes. This protein, encoded by the YKL004W gene, is essential for fungal viability and contributes to maintaining membrane integrity and signaling pathways in yeast. AUR1 is not a therapeutic target in humans, as it is absent in mammalian cells, making it relevant primarily for antifungal drug discovery rather than human diseases. The protein confers resistance to aureobasidin A, a cyclic lipopeptide antifungal that specifically inhibits its enzymatic activity, highlighting its role in fungal-specific lipid metabolism. Structural predictions from AlphaFold and domain analyses reveal conserved motifs typical of glycosyltransferases involved in lipid modification. Note that AUR1 should not be confused with aurora kinases (e.g., Arabidopsis thaliana AUR1, a serine/threonine-protein kinase), as it is a distinct fungal enzyme. Overall, AUR1 exemplifies a fungal-specific target exploited for selective antifungal agents without human off-target effects.

Other names

Aureobasidin A resistance proteinIPC synthase catalytic subunit AUR1

Inhibition of inositol phosphorylceramide synthase activity