title: Possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus.
abstract: Nordihydroguaiaretic acid (NDGA) caused disassembly of the Golgi apparatus of NRK cells in a dose-, time-, and energy-dependent manner but not in a microtubule-dependent manner. In contrast to brefeldin A, NDGA did not cause release of beta-COP, a component of Golgi-derived vesicles. However, NDGA-induced disassembly was blocked by AlF4-, an activator of the heterotrimeric but not the small GTP-binding proteins. In digitonin-permeabilized cells, guanosine 5'-3-O-(thio)triphosphate (GTPgammaS) as well as AlF4- blocked the NDGA-promoted disassembly of the Golgi apparatus, and Gbetagamma (betagamma subunits of heterotrimeric G proteins) reversed this effect. Our present results suggest the possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus.
authors.affiliation: Division of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka 812-82, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Yamaguchi
authors.forename: A
authors.initials: A
authors.lastname: Yamamoto
authors.forename: A
authors.initials: A
authors.lastname: Furuno
authors.forename: K
authors.initials: K
authors.lastname: Hatsuzawa
authors.forename: K
authors.initials: K
authors.lastname: Tani
authors.forename: M
authors.initials: M
authors.lastname: Himeno
authors.forename: M
authors.initials: M
authors.lastname: Tagaya
mesh_terms: D000818:Animals; D002460:Cell Line; D002463:Cell Membrane Permeability; D002772:Cholera Toxin / Q000494:pharmacology; D020756:Coatomer Protein; D003513:Cycloheximide / Q000494:pharmacology; D004072:Digitonin; D019204:GTP-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D006056:Golgi Apparatus / Q000187:drug effects / Q000502:physiology* / Q000648:ultrastructure; D016244:Guanosine 5'-O-(3-Thiotriphosphate) / Q000494:pharmacology; D007668:Kidney; D046911:Macromolecular Substances; D009637:Masoprocol / Q000494:pharmacology; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000032:analysis / Q000378:metabolism; D008870:Microtubules / Q000187:drug effects / Q000502:physiology / Q000648:ultrastructure; D051381:Rats; D010566:Virulence Factors, Bordetella / Q000494:pharmacology
chemical_list: D020756:Coatomer Protein; D046911:Macromolecular Substances; D008565:Membrane Proteins; D008869:Microtubule-Associated Proteins; D010566:Virulence Factors, Bordetella; D016244:Guanosine 5'-O-(3-Thiotriphosphate); D009637:Masoprocol; D002772:Cholera Toxin; D003513:Cycloheximide; D019204:GTP-Binding Proteins; D004072:Digitonin