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¹ Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, TN 37232
² Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232

Address correspondence to Kathleen L. Gould, Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, B2309 MCN, 1161 21st Ave. South, Nashville, TN 37232. Tel.: (615) 343-9502. Fax: (615) 343-0723. email: kathy.gould{at}vanderbilt.edu

Cytokinetic actin ring (CAR) formation in Schizosaccharomyces pombe requires two independent actin nucleation pathways, one dependent on the Arp2/3 complex and another involving the formin Cdc12p. Here we investigate the role of the S. pombe Cdc15 homology family protein, Cdc15p, in CAR assembly and find that it interacts with proteins from both of these nucleation pathways. Cdc15p binds directly to the Arp2/3 complex activator Myo1p, which likely explains why actin patches and the Arp2/3 complex fail to be medially recruited during mitosis in cdc15 mutants. Cdc15p also binds directly to Cdc12p. Cdc15p and Cdc12p not only display mutual dependence for CAR localization, but also exist together in a ring-nucleating structure before CAR formation. The disruption of these interactions in cdc15 null cells is likely to be the reason for their complete lack of CARs. We propose a model in which Cdc15p plays a critical role in recruiting and coordinating the pathways essential for the assembly of medially located F-actin filaments and construction of the CAR.

Key Words: S. pombe; cytokinesis; cell cycle; actin; cdc15

Abbreviations used in this paper: CAR, cytokinetic actin ring; FH3, formin homology 3; MBP, maltose binding protein; PCH, pombe Cdc15 homology; SH3, Src homology 3.

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