Regulation of the Golgi complex by phospholipid remodeling enzymes

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• 作者：Kevin D. Ha¹ ; Benjamin A. Clarke¹ ; William J. Brown ; ^{wjb5@cornell.edu}
• 关键词：AA ; Arachidonic acid ; ACAT ; acyl-CoA cholesterol acyltransferase ; AGPAT ; 1-acylglycerol-3-phosphate acyltransferase ; Arf ; ADP-ribosylating factor ; BARS ; BFA-inhibited ; ADP-ribosylated substrate ; BFA ; Brefeldin A ; CPT1 ; Choline-phosphotransferase ; DAG ; Dia
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular and Cell Biology of Lipids
• 出版年：2012
• 期刊代码：18_13881981
• 类别：bio
• 出版时间：August, 2012
• 卷：1821
• 期：8
• 页码：1078-1088
• 文件大小：1072 K

摘要

The mammalian Golgi complex is a highly dynamic organelle consisting of stacks of flattened cisternae with associated coated vesicles and membrane tubules that contribute to cargo import and export, intra-cisternal trafficking, and overall Golgi architecture. At the morphological level, all of these structures are continuously remodeled to carry out these trafficking functions. Recent advances have shown that continual phospholipid remodeling by phospholipase A (PLA) and lysophospholipid acyltransferase (LPAT) enzymes, which deacylate and reacylate Golgi phospholipids, respectively, contributes to this morphological remodeling. Here we review the identification and characterization of four cytoplasmic PLA enzymes and one integral membrane LPAT that participate in the dynamic functional organization of the Golgi complex, and how some of these enzymes are integrated to determine the relative abundance of COPI vesicle and membrane tubule formation.

This article is part of a Special Issue entitled Lipids and Vesicular Transport.