Journal
FEBS LETTERS
Volume 579, Issue 20, Pages 4383-4388Publisher
WILEY
DOI: 10.1016/j.febslet.2005.06.079
Keywords
ceramide kinase; ceramide; ceramide-1-phosphate; pleckstrin homology domain
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Ceramide kinase (CERK) converts ceramide (Cer) to ceramide-1-phosphate (C1P), a newly recognized bioactive molecule capable of regulating diverse cellular functions. The N-terminus of the CERK protein encompasses a sequence motif known as a pleckstrin homology (PH) domain. However, little is known regarding the functional roles of this domain in CERK. In this study, we have demonstrated that the PH domain of CERK is essential for its enzyme activity. Using site-directed mutagenesis, we have further determined that Leu10 in the PH domain has an important role in CERK activity. Replacing this residue with a neutral alanine or isoleucine, caused a dramatic decrease in CERK activity to 1% and 29%, respectively, compared to CERK, but had no effect on substrate affinity. The study presented here suggests that the PH domain of CERK is not only indispensable for its activity but also act as a regulator of CERK activity. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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