Structural highlights
Function
SAMD8_HUMAN Sphingomyelin synthases synthesize sphingolipids through transfer of a phosphatidyl head group on to the primary hydroxyl of ceramide. SAMD8 is an endoplasmic reticulum (ER) transferase that has no sphingomyelin synthase activity but can convert phosphatidylethanolamine (PE) and ceramide to ceramide phosphoethanolamine (CPE) albeit with low product yield. Appears to operate as a ceramide sensor to control ceramide homeostasis in the endoplasmic reticulum rather than a converter of ceramides. Seems to be critical for the integrity of the early secretory pathway.[1]
References
- ↑ Vacaru AM, Tafesse FG, Ternes P, Kondylis V, Hermansson M, Brouwers JF, Somerharju P, Rabouille C, Holthuis JC. Sphingomyelin synthase-related protein SMSr controls ceramide homeostasis in the ER. J Cell Biol. 2009 Jun 15;185(6):1013-27. PMID:19506037 doi:10.1083/jcb.200903152
