Phospholipase D2 is involved in the formation of Golgi tubules and ArfGAP1 recruitment

• Published in: PloS one Vol. 9; no. 10; p. e111685
• Main Authors: Martínez-Martínez, Narcisa, Martínez-Alonso, Emma, Ballesta, José, Martínez-Menárguez, José A
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 29.10.2014; Public Library of Science (PLoS)
• Subjects: Acids; Analysis; Biology; Biology and Life Sciences; Brefeldin A; Depletion; Employee recruitment; Endoplasmic reticulum; Enzymatic activity; Enzymes; Golgi apparatus; GTPase-Activating Proteins - genetics; GTPase-Activating Proteins - metabolism; HeLa Cells; Histology; Humans; Kinases; Lipids; Low temperature; Medical schools; Membranes; Molecular modelling; Overexpression; Phosphatidic acid; Phosphatidic Acids - metabolism; Phospholipase; Phospholipase D - antagonists & inhibitors; Phospholipase D - genetics; Phospholipase D - metabolism; Phospholipase D2; Phospholipases; Physiological aspects; Protein Transport; Proteins; Recruitment; Regulation; trans-Golgi Network - metabolism; Transport; Tubules; Spain
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0111685

Lipids and lipid-modifying enzymes play a key role in the biogenesis, maintenance and fission of transport carriers in the secretory and endocytic pathways. In the present study we demonstrate that phosphatidic acid generated by phospholipase D2 (PLD2) is involved in the formation of Golgi tubules. The main evidence to support this is: 1) inhibitors of phosphatidic acid formation and PLD2 depletion inhibit the formation of tubules containing resident enzymes and regulators of intra-Golgi transport in a low temperature (15°C) model of Golgi tubulation but do not affect brefeldin A-induced tubules, 2) inhibition of PLD2 enzymatic activity and PLD2 depletion in cells cultured under physiological conditions (37°C) induce the formation of tubules specifically containing Golgi matrix proteins, and, 3) over-expression of PLD2 induces the formation of a tubular network. In addition, it was found that the generation of this lipid by the isoenzyme is necessary for ArfGAP1 recruitment to Golgi membranes. These results suggest that both proteins are involved in the molecular mechanisms which drive the formation of different types of Golgi tubules.