Regulation of the Golgi structure by the α subunits of heterotrimeric G proteins

FEBS Letters

Itoh, Hiroshi¹  Tani, Katsuko²  Hatsuzawa, Kiyotaka²  Nagahama, Masami²  Tagaya, Mitsuo²  Yamaguchi, Tomohiro² 

[1] Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Kanagawa 226-8501, Japan;School of Life Science, Tokyo University of Pharmacy and Life Science, Horinouchi 1432-1, Hachioji, Tokyo 192-0392, Japan

关键词: Heterotrimeric G protein;    Golgi apparatus;    Nordihydroguaiaretic acid;    Vesicular transport;    ER;    endoplasmic reticulum;    BFA;    brefeldin A;    COPI;    coat protein I;    Man II;    mannosidase II;    NDGA;    nordihydroguaiaretic acid;    VSVG-GFP;    green fluorescent protein-tagged glycoprotein of vesicular stomatitis virus ts045;   

DOI  :  10.1016/S0014-5793(00)01284-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Gα_z or Gα_i2 significantly suppresses the disassembly of the Golgi apparatus induced by NDGA. Overexpression of Gβ₁γ₂, on the other hand, had no effect on NDGA-induced Golgi disassembly. Gα_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 α subunits of heterotrimeric G proteins are responsible for the maintenance of the Golgi structure.

【 授权许可】

Unknown