Regulation of Golgi structure and secretion by receptor-induced G protein βγ complex translocation Article (Web of Science)


  • We show that receptor induced G protein βγ subunit translocation from the plasma membrane to the Golgi allows a receptor to initiate fragmentation and regulate secretion. A lung epithelial cell line, A549, was shown to contain an endogenous translocating G protein γ subunit and exhibit receptor-induced Golgi fragmentation. Receptor-induced Golgi fragmentation was inhibited by a shRNA specific to the endogenous translocating γ subunit. A kinase defective protein kinase D and a phospholipase C β inhibitor blocked receptor-induced Golgi fragmentation, suggesting a role for this process in secretion. Consistent with βγ translocation dependence, fragmentation induced by receptor activation was inhibited by a dominant negative nontranslocating γ3. Insulin secretion was shown to be induced by muscarinic receptor activation in a pancreatic β cell line, NIT-1. Induction of insulin secretion was also inhibited by the dominant negative γ3 subunit consistent with the Golgi fragmentation induced by βγ complex translocation playing a role in secretion.


  • Saini, Deepak Kumar
  • Angaswamy, Nataraju
  • Saini, Deepti
  • Cho, Joon-Ho
  • Kalyanaraman, Vani
  • Gautam, Narasimhan

publication date

  • 2010

number of pages

  • 5

start page

  • 11417

end page

  • 11422


  • 107


  • 25