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The yeast acylglycerol acyltransferase LCA1 is a key component of Lands cycle for phosphatidylcholine turnover
Authors:Chen Qilin  Kazachkov Michael  Zheng Zhifu  Zou Jitao
Affiliation:Plant Biotechnology Institute, National Research Council Canada, 110 Gymnasium Place, Saskatoon, SK, Canada.
Abstract:
Cellular phospholipids undergo deacylation and reacylation through a process known as Lands cycle. In this report, we provide evidence demonstrating that yeast YOR175c, herein designated as LCA1, encodes a key component of the Lands cycle, the acyl-CoA: lysophosphatidylcholine acyltransferase (LPCAT). Deletion of LCA1 resulted in a drastic reduction in LPCAT activity, while over expression led to a several fold increase in enzyme activity. We further show that disruption of LCA1 caused an enhanced production of glycerophosphorylcholine, a product of phosphatidylcholine (PC) deacylation and that the lysophosphatidic acid acyltransferase SLC1 was not involved in this process. Identification of LCA1 provides an essential molecular tool for further study of Lands cycle in PC turnover.
Keywords:PC, Phosphatidylcholine   CDP-choline, cytidine 5′-diphosphocholine   DAG, diacylglycerol   LPCAT, acyl-CoA: lysophosphatidylcholine acyltransferase   LPAAT, acyl-CoA: lysophosphatidic acid acyltransferase   EUROSCARF, European Saccharoymces cerevisiae archive for functional analysis   DTT, dithiothreitol   PAF, platelet-activating factor   TCA, trichloroacetic acid   MBOAT, membrane-bound O-acyltransferase   LPA, lysophosphatidic acid   LPC, lysophosphatidylcholine   LPE, lysophosphatidylethanolamine   LPG, lysophosphatidylglycerol   LPI, lysophosphatidylinositol   GroPC, glycerophosphorylcholine
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