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Publication : MuLK, a eukaryotic multi-substrate lipid kinase.

First Author  Waggoner DW Year  2004
Journal  J Biol Chem Volume  279
Issue  37 Pages  38228-35
PubMed ID  15252046 Mgi Jnum  J:92836
Mgi Id  MGI:3054595 Doi  10.1074/jbc.M405932200
Citation  Waggoner DW, et al. (2004) MuLK, a eukaryotic multi-substrate lipid kinase. J Biol Chem 279(37):38228-35
abstractText  We report the identification and characterization of a novel lipid kinase that phosphorylates multiple substrates. This enzyme, which we term MuLK for multi-substrate lipid kinase, does not belong to a previously described lipid kinase family. MuLK has orthologs in many organisms and is broadly expressed in human tissues. Although predicted to be a soluble protein, MuLK co-fractionates with membranes and localizes to an internal membrane compartment. Recombinant MuLK phosphorylates diacylglycerol, ceramide, and 1-acylglycerol but not sphingosine. Although its affinity for diacylglycerol and ceramide are similar, MuLK exhibits a higher V(max) toward diacylglycerol in vitro, consistent with it acting primarily as a diacylglycerol kinase. MuLK activity was inhibited by sphingosine and enhanced by cardiolipin. It was stimulated by calcium when magnesium concentrations were low and inhibited by calcium when magnesium concentrations were high. The effects of charged lipids and cations on MuLK activity in vitro suggest that its activity in vivo is tightly regulated by cellular conditions.
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