RRC ID 39542
Author Yamaguchi T, Nagahama M, Itoh H, Hatsuzawa K, Tani K, Tagaya M.
Title Regulation of the golgi structure by the alpha subunits of heterotrimeric G proteins.
Journal FEBS Lett
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.
Volume 470(1)
Pages 25-8
Published 2000-3-17
DOI 10.1016/s0014-5793(00)01284-9
PII S0014-5793(00)01284-9
PMID 10722839
MeSH Animals Biological Transport Brefeldin A / pharmacology Cell Line Cell Membrane / metabolism Cyclooxygenase Inhibitors / pharmacology Endoplasmic Reticulum / metabolism GTP-Binding Protein alpha Subunit, Gi2 GTP-Binding Protein alpha Subunits* GTP-Binding Protein alpha Subunits, Gi-Go* Golgi Apparatus / drug effects Golgi Apparatus / physiology* Heterotrimeric GTP-Binding Proteins / biosynthesis Heterotrimeric GTP-Binding Proteins / genetics Heterotrimeric GTP-Binding Proteins / physiology* Masoprocol / pharmacology Nocodazole / pharmacology Protein Synthesis Inhibitors / pharmacology Proto-Oncogene Proteins / biosynthesis Proto-Oncogene Proteins / genetics Proto-Oncogene Proteins / physiology*
IF 3.057
Times Cited 12
WOS Category BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
Human and Animal Cells