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Originally published as MBC in Press, 10.1091/mbc.E03-05-0329 on October 31, 2003

Vol. 15, Issue 2, 435-446, February 2004

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DWWA, a Novel Protein Containing Two WW Domains and an IQ Motif, Is Required for Scission of the Residual Cytoplasmic Bridge during Cytokinesis in Dictyostelium

Akira Nagasaki *, and Taro Q.P. Uyeda

Gene Function Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8562, Japan

Submitted May 26, 2003; Revised August 9, 2003; Accepted September 30, 2003
Monitoring Editor: Peter Devreotes

We have identified a novel gene, dwwA, which is required for cytokinesis of Dictyostelium cells on solid surfaces. Its product, Dd WW domain containing protein A (DWWA), contains several motifs, including two WW domains, an IQ motif, a C2 domain, and a proline-rich region. On substrates, cells lacking dwwA were multinucleated and larger and flatter than wild-type cells due to their frequent inability to sever the cytoplasmic bridge connecting daughter cells after mitosis. When cultured in suspension, however, dwwA-null cells seemed to carry out cytokinesis normally via a process not driven by the shearing force arising from agitation of the culture. GFP-DWWA localized to the cell cortex and nucleus; analysis of the distributions of various truncation mutants revealed that the N-terminal half of the protein, which contains the C2 domain, is required for the cortical localization of DWWA. The IQ motif of DWWA binds calmodulin in vitro. Given that the scission process is also defective in calmodulin knockdown cells cultured on substrates (Liu et al., 1992), we propose that DWWA's multiple binding domains enable it to function as an adaptor protein, facilitating the scission process through the regulation of Ca2+/calmodulin-mediated remodeling of the actin cytoskeleton and/or modulation of membrane dynamics.


Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E03-05-0329. Article and publication date are available at www.molbiolcell.org/cgi/doi/10.1091/mbc.E03-05-0329.

* Corresponding author. E-mail address: a-nagasaki{at}aist.go.jp.




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PNAS, May 17, 2005; 102(20): 7186 - 7191.
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