In this report we have studied the morphological changes of the Golgi compl
ex (GC) that specifically accompany F-actin reorganizations. In starved rat
RBL-2H3 tumor mast cells, the GC, that was visualized at immunofluorescenc
e level with antibodies raised against the Golgi-resident proteins giantin,
mannosidase II, or TGN-38, showed a compacted morphology with a supranucle
ar positioning. Concomitant to membrane ruffle formation induced by epiderm
al growth factor (EGF) or phorbol 12-myristate 13-acetate (PMA), and stress
fiber formation induced by lysophosphatidic acid (LPA), specific GC morpho
logical changes were observed. When cells were stimulated with EGF or PMA,
the compacted GC morphology was transformed into a reticular network that w
as extended towards the cell periphery. When cells were incubated with LPA,
the GC acquired a characteristic ring-shaped morphology. Brefeldin A (BFA)
did not affect the PMA- or LPA-induced membrane ruffling and stress fiber
formation, respectively, indicating that actin rearrangements occurred inde
pendent of the presence of the GC. Upon BFA removal, the presence of PMA or
LPA during the recovery process induced the GC to acquire the morphologica
l appearance described above for each agent. Moreover, the PMA- but not the
LPA-induced GC rearrangements were sensitive to the actin perturbing agent
s cytochalasin D and jasplakinolide. When cells were preincubated with the
phosphatidylinositide 3-kinase (PI3K) inhibitors wortmannin or LY294002, th
e PMA-induced GC morphological changes were inhibited but not membrane ruff
les. Finally, the PMA-induced increase in the post-Golgi transport of glyco
saminoglycans to the cell surface was not altered by cytochalasin D or jasp
lakinolide. Altogether, these data suggest that: (1) the shape of the GC is
influenced by the 3D arrangement of actin microfilaments; (2) PI3K regulat
es the association of the GC with actin microfilaments; and (3) actin micro
filaments are not essential for the post-Golgi transport to the plasma memb
rane. Cell Motil. Cytoskeleton 43:334-348, 1999. (C) 1999 Wiley-Liss, Inc.