Ceramide 1-phosphate

Abstract

Over the past couple of decades, ceramide (Cer) has emerged as a lipid mediator of cell signaling in a variety of events, including apoptosis and cell differentiation, and its intracellular levels are tightly controlled. Several enzymes are known to be regulators of Cerlevels. One of these, ceramide kinase (CERK), catalyzes the conversion of ceramide (Cer) to ceramide 1-phosphate (C1P). Although the activity of this enzyme was reported in 1989, the CERK-gene was only recently identified. CERK, which is activated by Ca2+, possesses a typical diacylglycerol kinase catalytic domain, a pleckstrin homology domain, and a Ca2+/CaM binding domain. The groups that examined CERK/C1P functions suggested that CERK/C1P is involved in many processes including: membrane fusion, inflammation, DNA-synthesis, intracellular Ca2+ increase, and other processes. These CERK/C1P functions and the investigations over of the past decade that revealed them are reviewed here. © Springer-Verlag Tokyo 2006. All rights reserved.