Abstract:
:Ceramide kinase (CERK) converts ceramide to ceramide-1-phosphate (C1P), which has recently emerged as a new 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. Although the PH domain was previously demonstrated to be an important domain for the subcellular localization of CERK, the precise properties of this domain remained unclear. In this study, we reveal that the PH domain of CERK exhibits high affinity for phosphatidylinositol 4,5-bisphosphate (PI(4,5)P(2)), among other lipids. Furthermore, in COS7 cells, GFP-fused CERK translocated rapidly from the cytoplasm to the plasma membrane in response to hyper-osmotic stress, which is known to increase the intracellular PI(4,5)P(2) levels, whereas a PH domain deletion mutant did not. Additionally, in [(32)P]orthophosphate-labeled COS7 cells, the translocation of CERK to the plasma membrane induced a 2.8-fold increase in C1P levels. The study presented here provides insight into the crucial role of the CERK-PH domain in plasma membrane targeting, through its binding to PI(4,5)P(2), and subsequent induction of C1P production in the vicinity of the membrane.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kim TJ,Mitsutake S,Igarashi Ydoi
10.1016/j.bbrc.2006.01.170subject
Has Abstractpub_date
2006-04-07 00:00:00pages
611-7issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(06)00253-1journal_volume
342pub_type
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