Reference - Detail
RRC ID | 38978 |
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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) |