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The interaction between the pleckstrin homology domain of ceramide kinase and phosphatidylinositol 4,5-bisphosphate regulates the plasma membrane targeting and ceramide 1-phosphate levels

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/8409

Title: The interaction between the pleckstrin homology domain of ceramide kinase and phosphatidylinositol 4,5-bisphosphate regulates the plasma membrane targeting and ceramide 1-phosphate levels
Authors: Kim, Tack-Joong Browse this author
Mitsutake, Susumu Browse this author →KAKEN DB
Kato, Mariko Browse this author
Igarashi, Yasuyuki Browse this author →KAKEN DB
Keywords: Ceramide kinase
Ceramide
Ceramide 1-phosphate
Pleckstrin homology domain
PI(4,5)P2
Issue Date: 7-Apr-2006
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 342
Issue: 2
Start Page: 611
End Page: 617
Publisher DOI: 10.1016/j.bbrc.2006.01.170
PMID: 16488390
Abstract: Ceramide kinase (CERK) converts ceramide (Cer) 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)P2)[0], among other lipids. Furthermore, in COS7 cells, GFPfused 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)P2 levels, whereas a PH-domain deletion mutant did not. Additionally, in [32P]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[0]-PH domain in plasma membrane targeting, through its binding to PI(4,5)P2, and subsequent induction of C1P production in the vicinity of the membrane
Relation: http://www.sciencedirect.com/science/journal/0006291X
Type: article (author version)
URI: http://hdl.handle.net/2115/8409
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 光武 進

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