title: Lysophosphatidic acid acyltransferase 3 regulates Golgi complex structure and function.
abstract: Recent studies have suggested that the functional organization of the Golgi complex is dependent on phospholipid remodeling enzymes. Here, we report the identification of an integral membrane lysophosphatidic acid-specific acyltransferase, LPAAT3, which regulates Golgi membrane tubule formation, trafficking, and structure by altering phospholipids and lysophospholipids. Overexpression of LPAAT3 significantly inhibited the formation of Golgi membrane tubules in vivo and in vitro. Anterograde and retrograde protein trafficking was slower in cells overexpressing LPAAT3 and accelerated in cells with reduced expression (by siRNA). Golgi morphology was also dependent on LPAAT3 because its knockdown caused the Golgi to become fragmented. These data are the first to show a direct role for a specific phospholipid acyltransferase in regulating membrane trafficking and organelle structure.
authors.affiliation: Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
authors.forename: John A
authors.initials: JA
authors.lastname: Schmidt
authors.forename: William J
authors.initials: WJ
authors.lastname: Brown
mesh_terms: D008243:1-Acylglycerophosphocholine O-Acyltransferase / Q000235:genetics / Q000378:metabolism*; D000217:Acyltransferases / Q000235:genetics / Q000378:metabolism*; D000813:Anilides / Q000378:metabolism; D000818:Animals; D020126:Brefeldin A / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000378:metabolism; D006056:Golgi Apparatus / Q000201:enzymology* / Q000648:ultrastructure; D006367:HeLa Cells; D006801:Humans; D007425:Intracellular Membranes / Q000201:enzymology* / Q000648:ultrastructure; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D050356:Lipid Metabolism; D008246:Lysophospholipids / Q000378:metabolism; D037241:Mannose-Binding Lectins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D011500:Protein Synthesis Inhibitors / Q000378:metabolism; D021381:Protein Transport / Q000502:physiology; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D051381:Rats; D021601:trans-Golgi Network / Q000378:metabolism / Q000648:ultrastructure
chemical_list: D000813:Anilides; D004791:Enzyme Inhibitors; D007527:Isoenzymes; C084004:LMAN1 protein, human; D008246:Lysophospholipids; D037241:Mannose-Binding Lectins; D008565:Membrane Proteins; D011500:Protein Synthesis Inhibitors; D034741:RNA, Small Interfering; C069304:PD 128042; D020126:Brefeldin A; D000217:Acyltransferases; D008243:1-Acylglycerophosphocholine O-Acyltransferase; C018764:2-acylglycerophosphate acyltransferase; C032881:lysophosphatidic acid