CERK
Ceramide kinase (CERK) is the only known mammalian enzyme that phosphorylates ceramide, producing the sphingolipid mediator ceramide-1-phosphate (C1P). Its architecture features an N-terminal CBL domain that binds phosphoinositides and targets the enzyme to the trans-Golgi network and plasma membrane, adjacent to a catalytic domain related to the diacylglycerol kinase fold. CERK activity requires calcium and is stimulated by membrane interaction. C1P promotes cell survival, proliferation and inflammatory responses, regulates phospholipase A2 and membrane-trafficking events, and has been implicated in macrophage function, tumor growth and metastasis, marking CERK as an emerging node in sphingolipid signaling.
