RRC ID 38978
Author Yamaguchi T, Yamamoto A, Furuno A, Hatsuzawa K, Tani K, Himeno M, Tagaya M.
Title Possible involvement of heterotrimeric G proteins in the organization of the Golgi apparatus.
Journal J Biol Chem
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.
Volume 272(40)
Pages 25260-6
Published 1997-10-3
DOI 10.1074/jbc.272.40.25260
PII S0021-9258(19)63540-4
PMID 9312142
MeSH Animals Cell Line Cell Membrane Permeability Cholera Toxin / pharmacology Coatomer Protein Cycloheximide / pharmacology Digitonin GTP-Binding Proteins / chemistry* GTP-Binding Proteins / metabolism* Golgi Apparatus / drug effects Golgi Apparatus / physiology* Golgi Apparatus / ultrastructure Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology Kidney Macromolecular Substances Masoprocol / pharmacology Membrane Proteins / analysis Membrane Proteins / metabolism Microtubule-Associated Proteins / analysis Microtubule-Associated Proteins / metabolism Microtubules / drug effects Microtubules / physiology Microtubules / ultrastructure Rats Virulence Factors, Bordetella / pharmacology
IF 4.238
Times Cited 37
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY
Resource
Human and Animal Cells NRK(RCB0043)