Interplay of SLC33A1-dependent and -independent Golgi sialic acid O-acetylation in CASD1 catalysis - PubMed
6 hours ago
- #Sialic acid O-acetylation
- #CASD1
- #SLC33A1
- Sialic acid O-acetylation modulates sialoglycan recognition and ganglioside biology, catalyzed by the Golgi protein CASD1.
- The acetyl-CoA transporter SLC33A1 supplies acetyl-CoA to CASD1's luminal domain; its variants impair ganglioside 9-O-acetylation and are linked to neurodevelopmental disorders.
- SLC33A1 inactivation impairs di-O-acetylation but still allows mono-O-acetylation, revealing a second active site in CASD1 similar to HGSNAT.
- CASD1 has dual functionality: it catalyzes di-O-acetylation via SLC33A1-dependent luminal and SLC33A1-independent transmembrane acetylation.