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Vol. 10, Issue 6, 1763-1782, June 1999
Section of Biochemistry, Molecular, and Cell Biology, Cornell
University, Ithaca, New York 14853; and Although membrane tubules can be found extending from, and
associated with, the Golgi complex of eukaryotic cells, their
physiological function has remained unclear. To gain insight into the
biological significance of membrane tubules, we have developed methods
for selectively preventing their formation. We show here that a broad range of phospholipase A2 (PLA2) antagonists
not only arrest membrane tubule-mediated events that occur late in the
assembly of the Golgi complex but also perturb its normal steady-state
tubulovesicular architecture by inducing a reversible fragmentation
into separate "mini-stacks." In addition, we show that these same
compounds prevent the formation of membrane tubules from Golgi stacks
in an in vitro reconstitution system. This in vitro assay was further used to demonstrate that the relevant PLA2 activity
originates from the cytoplasm. Taken together, these results
demonstrate that Golgi membrane tubules, sensitive to potent and
selective PLA2 antagonists, mediate both late events in the
reassembly of the Golgi complex and the dynamic maintenance of its
steady-state architecture. In addition, they implicate a role for
cytoplasmic PLA2 enzymes in mediating these membrane
trafficking events.
Department of
Biological Sciences, Stanford University, Stanford, California 94305
These authors contributed equally.
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