Alternative splicing of UCP1 by non-cell-autonomous action of PEMT
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Johnson, Jordan M.
Verkerke, Anthony R.P.
Maschek, J. Alan
Ferrara, Patrick J.
Lin, Chien-Te
Kew, Kimberly A.
Neufer, P. Darrell
Lodhi, Irfan J.
Cox, James E.
Funai, Katsuhiko
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Abstract
Phosphatidylethanolamine methyltransferase (PEMT) generates phosphatidylcholine (PC), the most abundant phospholipid in the mitochondria and an important acyl chain donor for cardiolipin (CL) biosynthesis. Mice lacking PEMT (PEMTKO) are cold-intolerant when fed a high-fat diet (HFD) due to unclear mechanisms. The purpose of this study was to determine whether PEMT-derived phospholipids are important for the function of uncoupling protein 1 (UCP1) and thus for maintenance of core temperature.
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10.1016/j.molmet.2019.10.007