title: Membrane tubule-mediated reassembly and maintenance of the Golgi complex is disrupted by phospholipase A2 antagonists.
abstract: Although membrane tubules can be found extending from, and associated with, the Golgi complex of eukaryotic cells, their physiological function has remained unclear. To gain insight into the biological significance of membrane tubules, we have developed methods for selectively preventing their formation. We show here that a broad range of phospholipase A2 (PLA2) antagonists not only arrest membrane tubule-mediated events that occur late in the assembly of the Golgi complex but also perturb its normal steady-state tubulovesicular architecture by inducing a reversible fragmentation into separate "mini-stacks." In addition, we show that these same compounds prevent the formation of membrane tubules from Golgi stacks in an in vitro reconstitution system. This in vitro assay was further used to demonstrate that the relevant PLA2 activity originates from the cytoplasm. Taken together, these results demonstrate that Golgi membrane tubules, sensitive to potent and selective PLA2 antagonists, mediate both late events in the reassembly of the Golgi complex and the dynamic maintenance of its steady-state architecture. In addition, they implicate a role for cytoplasmic PLA2 enzymes in mediating these membrane trafficking events.
authors.affiliation: Section of Biochemistry, Molecular, and Cell Biology, Cornell University, Ithaca, New York 14853, USA.
authors.forename: P
authors.initials: P
authors.lastname: de Figueiredo
authors.forename: R S
authors.initials: RS
authors.lastname: Polizotto
authors.forename: D
authors.initials: D
authors.lastname: Drecktrah
authors.forename: W J
authors.initials: WJ
authors.lastname: Brown
mesh_terms: D062365:Aminobenzoates / Q000494:pharmacology; D000818:Animals; D020126:Brefeldin A / Q000494:pharmacology; D002474:Cell-Free System; D002478:Cells, Cultured; D002723:Chlorobenzoates; D002934:Cinnamates / Q000494:pharmacology; D020756:Coatomer Protein; D004721:Endoplasmic Reticulum / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006056:Golgi Apparatus / Q000187:drug effects / Q000378:metabolism* / Q000821:virology; D007425:Intracellular Membranes / Q000187:drug effects / Q000648:ultrastructure*; D008099:Liver / Q000166:cytology / Q000187:drug effects; D008565:Membrane Proteins / Q000187:drug effects / Q000378:metabolism; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure*; D010741:Phospholipases A / Q000037:antagonists & inhibitors*; D054467:Phospholipases A2; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D011809:Quinones / Q000494:pharmacology; D051381:Rats; D014721:Vesicular stomatitis Indiana virus / Q000378:metabolism; D062367:ortho-Aminobenzoates
chemical_list: D062365:Aminobenzoates; D002723:Chlorobenzoates; D002934:Cinnamates; D020756:Coatomer Protein; D004791:Enzyme Inhibitors; D008565:Membrane Proteins; D011500:Protein Synthesis Inhibitors; D011809:Quinones; D062367:ortho-Aminobenzoates; D020126:Brefeldin A; C067346:illimaquinone; C060048:2-(4-amylcinnamoyl)amino-4-chlorobenzoic acid; D010741:Phospholipases A; D054467:Phospholipases A2