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Vol. 12, Issue 5, 1367-1380, May 2001

*Division of Biology, Department of Life Sciences, Graduate School
of Arts and Sciences, University of Tokyo, Tokyo, 153-8902, Japan; and
We characterized the novel Schizosaccharomyces pombe
genes myo4+ and
myo5+, both of which encode myosin-V heavy
chains. Disruption of myo4 caused a defect in cell
growth and led to an abnormal accumulation of secretory vesicles
throughout the cytoplasm. The mutant cells were rounder than normal,
although the sites for cell polarization were still established.
Elongation of the cell ends and completion of septation required more
time than in wild-type cells, indicating that Myo4 functions in
polarized growth both at the cell ends and during septation. Consistent
with this conclusion, Myo4 was localized around the growing cell ends,
the medial F-actin ring, and the septum as a cluster of dot structures.
In living cells, the dots of green fluorescent protein-tagged Myo4
moved rapidly around these regions. The localization and movement of
Myo4 were dependent on both F-actin cables and its motor activity but
seemed to be independent of microtubules. Moreover, the motor activity of Myo4 was essential for its function. These results suggest that Myo4
is involved in polarized cell growth by moving with a secretory vesicle
along the F-actin cables around the sites for polarization. In
contrast, the phenotype of myo5 null cells was
indistinguishable from that of wild-type cells. This and other data
suggest that Myo5 has a role distinct from that of Myo4.
Department of Cell Biology, National Institute for Basic
Biology, Okazaki, 444-8585, Japan
Corresponding author. E-mail
address: mabuchi{at}ims.u-tokyo.ac.jp
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