Regulation of Golgi structure through heterotrimeric G proteins

Cell. 1997 Nov 28;91(5):617-26. doi: 10.1016/s0092-8674(00)80449-3.

Abstract

We have previously shown that ilimaquinone (IQ), a marine sponge metabolite, causes complete vesiculation of the Golgi stacks. By reconstituting the IQ-mediated vesiculation of the Golgi apparatus in permeabilized cells, we now demonstrate that this process does not require ARF and coatomers, which are necessary for the formation of Golgi-derived COPI vesicles. We find that IQ-mediated Golgi vesiculation is inhibited by G alpha(s)-GDP and G alpha(i3)-GDP. Interestingly, adding betagamma subunits in the absence of IQ is sufficient to vesiculate Golgi stacks. Our findings reveal that IQ-mediated Golgi vesiculation occurs through activation of heterotrimeric G proteins and that it is the free betagamma, and not the activated alpha subunit, that triggers Golgi vesiculation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cells, Cultured
  • Cytosol / chemistry
  • Cytosol / metabolism
  • Enzyme Inhibitors / pharmacology
  • GTP-Binding Protein alpha Subunits, Gs
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / drug effects
  • GTP-Binding Proteins / metabolism*
  • Golgi Apparatus / chemistry
  • Golgi Apparatus / metabolism*
  • Guanosine 5'-O-(3-Thiotriphosphate) / pharmacology
  • Guanosine Diphosphate / analogs & derivatives
  • Guanosine Diphosphate / pharmacology
  • Guanosine Triphosphate / analogs & derivatives
  • Guanosine Triphosphate / pharmacology
  • Intracellular Membranes / chemistry
  • Intracellular Membranes / metabolism
  • Kidney / cytology
  • Quinones / pharmacology
  • Rats
  • Signal Transduction / physiology

Substances

  • Enzyme Inhibitors
  • Quinones
  • Guanosine Diphosphate
  • Guanosine 5'-O-(3-Thiotriphosphate)
  • illimaquinone
  • Guanosine Triphosphate
  • GTP-Binding Proteins
  • GTP-Binding Protein alpha Subunits, Gs