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Novel Lipid Transfer Protein CPTP and its Fluorescent Substrate

Fluorescently labeled ceramide-1-phosphate synthesized in the Laboratory of lipid chemistry (IBCh RAS) permitted determination of a novel lipid transfer protein specificity.

Boldyrev I.A.

Ceramide-1-phosphate (C1P) activates cytosolic phospholipase A2, which produces arachidonic acid from phosphatidylcholine thus triggering production of eicosanoids — lipid mediators of many physiological processes. Time and place of eicosanoid production are strictly controlled. For this purpose, cells use lipid-specific transfer proteins. However, no protein that would transfer C1P has been known until recently, when an unknown lipid transfer protein gene has been revealed in the human genome. The new protein exhibited a modest 17% sequence similarity to a known glycolipid transfer protein. The substrate of the newly detected protein was unknown. Julian Molotkovsky of the Laboratory of lipid chemistry (IBCh RAS) synthesized a set of fluorescently labeled lipids of various structures that was used to prove C1P was a substrate of the transfer protein and study the kinetics of the transfer. This work became a part of a larger project that joined researchers from the US, Spain, and Russia, in determination of C1P transfer protein structure, specificity, and details of interactions with its substrate.

Simanshu D.K., Kamlekar R.K., Wijesinghe D.S., Zou X., Zhai X., Mishra S.K., Molotkovsky J.G., Malinina L., Hinchcliffe E.H., Chalfant C.E., Brown R.E., Patel D.J. (2013). Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids. Nature 500, 463–467.

december 15, 2013

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