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Vol. 13, Issue 2, 515-529, February 2002
and
*The Institute of Molecular Agrobiology, The National University of
Singapore, Singapore 117604, Republic of Singapore; and
Schizosaccharomyces pombe cells divide by medial
fission through the use of an actomyosin-based contractile ring. A
mulitlayered division septum is assembled in concert with ring
constriction. Finally, cleavage of the inner layer of the division
septum results in the liberation of daughter cells. Although numerous
studies have focused on actomyosin ring and division septum assembly, little information is available on the mechanism of cell separation. Here we describe a mutant, sec8-1, that is defective in
cell separation but not in other aspects of cytokinesis.
sec8-1 mutants accumulate ~100-nm vesicles and have
reduced secretion of acid phosphatase, suggesting that they are
defective in exocytosis. Sec8p is a component of the exocyst complex.
Using biochemical methods, we show that Sec8p physically interacts with
other members of the exocyst complex, including Sec6p, Sec10p, and
Exo70p. These exocyst proteins localize to regions of active
exocytosisDepartment of Molecular Genetics and Microbiology, The
University of Massachusetts Medical Center, Worcester, Massachusetts
01605
at the growing ends of interphase cells and in the medial
region of cells undergoing cytokinesisin an F-actin-dependent and
exocytosis-independent manner. Analysis of a number of mutations in
various exocyst components has established that these components are
essential for cell viability. Interestingly, all exocyst mutants
analyzed appear to be able to elongate and to assemble division septa
but are defective for cell separation. We therefore propose that the
fission yeast exocyst is involved in targeting of enzymes responsible
for septum cleavage. We further propose that cell elongation and
division septum assembly can continue with minimal levels of exocyst function.
Hongyan Wang and Xie Tang contributed equally to
this work.
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