Premium
Regulation of the Golgi structure by the α subunits of heterotrimeric G proteins
Author(s) -
Yamaguchi Tomohiro,
Nagahama Masami,
Itoh Hiroshi,
Hatsuzawa Kiyotaka,
Tani Katsuko,
Tagaya Mitsuo
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01284-9
Subject(s) - heterotrimeric g protein , golgi apparatus , brefeldin a , microbiology and biotechnology , nocodazole , nordihydroguaiaretic acid , g protein , chemistry , protein subunit , biochemistry , biology , endoplasmic reticulum , signal transduction , lipoxygenase , enzyme , cell , cytoskeleton , gene
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 Gβ 1 γ 2 , 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.