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MBC in Press, published online ahead of print February 6, 2004
Mol. Biol. Cell 10.1091/mbc.E03-09-0644

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Submitted on September 10, 2003
Revised on November 30, 2003
Accepted on January 11, 2004

Inhibition of Membrane Tubule Formation and Trafficking by Isotetrandrine, an Antagonist of G-protein Regulated Phospholipase A2 Enzymes

Diane Chan1, Marian Strang1, Bret Judson1, and William J. Brown1*

1 Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 18483

* Corresponding author. E-mail address: wjb5{at}cornell.edu.

Previous studies have established a role for cytoplasmic phospholipase A2 (PLA2) activity in tubule-mediated retrograde trafficking between the Golgi complex and the endoplasmic reticulum (ER). However, little else is known about how membrane tubule formation is regulated. This study demonstrates that isotetrandrine (ITD), a biscoclaurine alkaloid known to specifically inhibit PLA2 enzyme activation by heterotrimeric G-proteins, effectively prevented brefeldin A (BFA)-induced tubule formation from the Golgi complex and retrograde trafficking to the ER. In addition, ITD inhibited BFA-stimulated tubule formation from the trans Golgi network and endosomes. ITD inhibition of the BFA response was potent (IC50 ~10-20 µM) and rapid (complete inhibition with a 10-15 min preincubation). ITD also inhibited normal retrograde trafficking as revealed by the formation of nocodazole-induced Golgi mini-stacks at ER exit sites. Treatment of cells with ITD alone caused the normally interconnected Golgi ribbons to become fragmented and dilated, but cisternae were still stacked and located in a juxtanuclear position. These results suggests that a G-protein-binding PLA2 enzyme plays a pivotal role in tubule mediated trafficking between the Golgi and the ER, the maintenance of the interconnected ribbons of Golgi stacks, and tubule formation from endosomes.




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