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© The Rockefeller University Press, 0021-9525/1997//169 $5.00
The Journal of Cell Biology, Volume 137, Number 1, , 1997 169-182

Article

cdc12p, a Protein Required for Cytokinesis in Fission Yeast, Is a Component of the Cell Division Ring and Interacts with Profilin



Fred Chang*,{ddagger}, David Drubin{ddagger}, and Paul Nurse*

* Imperial Cancer Research Fund, London WC2A 3PX, United Kingdom; and {ddagger} Department of Molecular and Cell Biology, University of California, Berkeley, California 94720-3202

As in many other eukaryotic cells, cell division in fission yeast depends on the assembly of an actin ring that circumscribes the middle of the cell. Schizosaccharomyces pombe cdc12 is an essential gene necessary for actin ring assembly and septum formation. Here we show that cdc12p is a member of a family of proteins including Drosophila diaphanous, Saccharomyces cerevisiae BNI1, and S. pombe fus1, which are involved in cytokinesis or other actin-mediated processes. Using indirect immunofluorescence, we show that cdc12p is located in the cell division ring and not in other actin structures. When overexpressed, cdc12p is located at a medial spot in interphase that anticipates the future ring site. cdc12p localization is altered in actin ring mutants. cdc8 (tropomyosin homologue), cdc3 (profilin homologue), and cdc15 mutants exhibit no specific cdc12p staining during mitosis. cdc4 mutant cells exhibit a medial cortical cdc12p spot in place of a ring. mid1 mutant cells generally exhibit a cdc12p spot with a single cdc12p strand extending in a random direction. Based on these patterns, we present a model in which ring assembly originates from a single point on the cortex and in which a molecular pathway for the functions of cytokinesis proteins is suggested. Finally, we found that cdc12 and cdc3 mutants show a syntheticlethal genetic interaction, and a proline-rich domain of cdc12p binds directly to profilin cdc3p in vitro, suggesting that one function of cdc12p in ring assembly is to bind profilin.

Abbreviations used in this paper: DAPI, 4',6-diamidino-2-phenylindole; ECL, enhanced chemiluminescence; GST, glutathione-S-transferase; PLP, poly-L-proline.

F. Chang was supported by the Helen Hay Whitney Foundation and a University of California CRCC grant.

Please address all correspondence to Fred Chang, Department of Microbiology, Columbia University, 701 West 168th Street, New York 10032. Fax: (212) 305-1468. e-mail: fc99{at}columbia.edu


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