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Updated: Jul 30, 2026

Measuring G-protein-coupled Receptor Signaling via Radio-labeled GTP Binding
Published on: June 9, 2017
Regulation of the golgi structure by the alpha subunits of heterotrimeric G proteins
T Yamaguchi1, M Nagahama, H Itoh
1School of Life Science, Tokyo University of Pharmacy and Life Science, Horinouchi 1432-1, Hachioji, Tokyo, Japan.
Abstract:
Disassembly of the Golgi apparatus is elicited by the action of nordihydroguaiaretic acid (NDGA) and this disassembly is prevented by the activation of heterotrimeric G proteins. In the present study we showed that overexpression of Galpha(z) or Galpha(i2) significantly suppresses the disassembly of the Golgi apparatus induced by NDGA. Overexpression of Gbeta(1)gamma(2), on the other hand, had no effect on NDGA-induced Golgi disassembly. Galpha(z) neither blocked Golgi disassembly induced by brefeldin A or nocodazole, nor interfered with protein transport, suggesting its specificity on the action of NDGA. Our results suggest that the alpha subunits of heterotrimeric G proteins are responsible for the maintenance of the Golgi structure.
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