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Vol. 11, Issue 5, 1727-1737, May 2000
and
*Department of Cell Biology and Physiology, Washington University,
St. Louis, Missouri 63110; and Departments of We examined the role of the actin cytoskeleton in secretion in
Saccharomyces cerevisiae with the use of several
quantitative assays, including time-lapse video microscopy of cell
surface growth in individual living cells. In latrunculin, which
depolymerizes filamentous actin, cell surface growth was completely
depolarized but still occurred, albeit at a reduced level. Thus,
filamentous actin is necessary for polarized secretion but not for
secretion per se. Consistent with this conclusion, latrunculin caused
vesicles to accumulate at random positions throughout the cell.
Cortical actin patches cluster at locations that correlate with sites
of polarized secretion. However, we found that actin patch polarization is not necessary for polarized secretion because a mutant,
bee1Cell
Biology and Molecular, Cellular, Developmental Biology
and Pathology, Yale University, New Haven, Connecticut 06520
(las17), which completely lacks actin patch
polarization, displayed polarized growth. In contrast, a mutant lacking
actin cables, tpm1-2 tpm2, had a severe defect in
polarized growth. The yeast class V myosin Myo2p is hypothesized to
mediate polarized secretion. A mutation in the motor domain of Myo2p,
myo2-66, caused growth to be depolarized but with only a
partial decrease in the level of overall growth. This effect is similar
to that of latrunculin, suggesting that Myo2p interacts with
filamentous actin. However, inhibition of Myo2p function by expression
of its tail domain completely abolished growth.
Online version of this article contains video
material for Figures 4 and 5. Online version available at
www.molbiolcell.org.
§
Corresponding author. E-mail address:
jcooper{at}cellbio.wustl.edu.
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