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Ceramide kinase

In enzymology, a ceramide kinase, also abbreviated as CERK, is an enzyme that catalyzes the chemical reaction:ATP + ceramide ADP + ceramide 1-phosphate

Gene
CERK is encoded by the CERK gene. The CERK gene is located on human chromosome 22q13, contains 13 exons, and is approximately 4.5kb in length. CERK shares sequence homology with sphingosine kinase type I, including an N-terminal pleckstrin homology (PH) domain and a diacylglycerol kinase domain. BLAST searches of expressed sequence tag (ESTs) by Sugiura and colleagues ==Protein==
Protein
CERK is a 537 amino acid enzyme in humans (531 in mice). Upon discovery, CERK was proposed to be a ceramide kinase that functions in the presence of μM concentration of calcium anions. Since CERK lacks a calcium binding site, the regulatory mechanism of CERK was poorly understood. CERK was later confirmed to bind calmodulin in the presence of calcium, indicating the calmodulin first binds calcium and then CERK. Once bound, CERK becomes active and is capable of phosphorylating ceramides. cerebrum granule cells, and epithelium-derived lung cells. When inactive, CERK is suspended within the cytosol of the cell. When CERK is activated by interleukin-1β, and from there, possibly delivered to the plasma membrane. Ceramide kinase has also been demonstrated to regulate localization and level of phosphatidylinositol 4,5-bisphosphate (PIP2) produced from NORPA, a phospholipase C homolog in Drosophila melanogaster. In addition to endosomal and trans-golgi localization, CERK has been found to localize to outer mitochondrial membrane at the site of COX-2 localization in A549 cells. ==Ceramide-1-phosphate==
Ceramide-1-phosphate
As a lipid kinase CERK is responsible for the phosphorylation of ceramides. CERK is capable of phosphorylating multiple ceramide species. Though CERK will phosphorylate C2, C20, C22, and C24 ceramides, substrate specificity is quite poor. By contrast, CERK has the greatest substrate specificity for C6, C8, and C16 ceramides, indicating that the location of the sphingosine group plays a role in specificity. Dihydroceramide can also be phosphorylated by CERK, but to a lesser extent. In contrast to C6 ceramide, CERK has low specificity for C6 dihydroceramide, but retains high specificity for C8 dihydroceramide- Ceramide transport proteins (CERTs) transport ceramides to CERK for phosphorylation. Phosphorylation of ceramides to produce ceramide-1-phosphate (C-1-P) is believed to facilitate the localization of cPLA2 to the trans-golgi so that CERK can activate cPLA2. ==Functions in molecular biology==
Functions in molecular biology
Cell survival and proliferation Production of C-1-P bolsters cell survival and proliferation. It has been shown that C-1-P promotes DNA synthesis in fibroblasts. C-1-P also prevents apoptosis by inhibiting the caspase-9/caspase-3 pathway and preventing DNA fragmentation in macrophages. This is thought to occur via C-1-P interacting with and blocking functionality of acid sphingomyelinase. This results in diminished ceramide production, which precludes apoptosis. Recently, phosphorylation of ceramide via CERK has been shown to stimulate myoblast proliferation. It was demonstrated that C-1-P perpetuates the phosphorylation of glycogen synthase kinase-3 β and retinoblastoma protein, which contributes to transition from the G1 phase to M phase of the cell cycle. Additionally, production of C-1-P appears to result in increased expression of Cyclin D. CERK has demonstrated an ability to activate phosphatidylinositol 3-kinase/Akt (PI3K/Akt), ERK1/2, and mTOR. Other roles In addition to cell survival and proliferation, CERK has been implicated in many other processes. CERK is believed to participate in altering the lipid raft structure via C-1-P production, contributing to phagosome formation in polymorphonuclear leukocytes. CERK has also been found to participate in the calcium-dependent degranulation of mast cells. ==References==
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