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J. Cell Biol.,
Volume 143, Number 2, October 19, 1998 415-427
Verna and Marrs McLean Department of Biochemistry, Baylor College of Medicine, Houston, Texas 77030
Cytokinesis is the part of the cell cycle in
which the cell is cleaved to form two daughter cells. The
unicellular yeast, Schizosaccharomyces pombe is an excellent model organism in which to study cell division,
since it shows the general features of eukaryotic cell division and is amenable to genetic analysis. In this manuscript we describe the isolation and characterization of
a new protein, imp2, which is required for normal septation in fission yeast. imp2, which colocalizes with the
medial ring during septation, is structurally similar to a
group of proteins including the S. pombe cdc15 and the
mouse PSTPIP that are localized to, and thought to be
involved in actin ring organization. Cells in which the
imp2 gene is deleted or overexpressed have septation and cell separation defects. An analysis of the actin cytoskeleton shows the lack of a medial ring in septating
cells that overexpress imp2, and the appearance of abnormal medial ring structures in septated cells that lack
imp2. These observations suggest that imp2 destabilizes
the medial ring during septation. imp2 also shows genetic interactions with several, previously characterized septation genes, strengthening the conclusion that it
plays a role in normal fission yeast septation.
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