Abstract
Many membrane processes occur in discrete membrane domains containing lipid rafts1, but little is known about how these domains are organized and positioned. In the fission yeast Schizosaccharomyces pombe, a sterol-rich membrane domain forms at the cell-division site2. Here, we show that formation of this membrane domain is independent of the contractile actin ring, septation, mid1p and the septins, and also requires cdc15p3, an essential contractile ring protein that associates with lipid rafts. cdc15 mutants have membrane domains in the shape of spirals. Overexpression of cdc15p in interphase cells induces abnormal membrane domain formation in an actin-independent manner. We propose that cdc15p functions to organize lipid rafts at the cleavage site for cytokinesis.
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Acknowledgements
We thank A. Berlin, R. Lustig and B. Enloe for technical support; V. Simanis, A. Chang, A. Pidoux, K. Gould, J. Pringle and P. Crews for valuable reagents; D. Burgess, M. Ng, B. Lauring, F. Maxfield, S. Mukherjee, P. Tran, B. Feierbach, A. Rafael, R. Daga, A. Yonetani and other members of our lab for discussion and advice. This work was supported by National Institutes of Health grant R01 GM056836 to F.C. and Postdoctoral Fellowships from TOYOBO Biotechnology Foundation and Uehara Memorial Foundation to T.T.
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Takeda, T., Kawate, T. & Chang, F. Organization of a sterol-rich membrane domain by cdc15p during cytokinesis in fission yeast. Nat Cell Biol 6, 1142–1144 (2004). https://doi.org/10.1038/ncb1189
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DOI: https://doi.org/10.1038/ncb1189
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