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在裂殖酵母胞质分裂过程中,cdc15p对富含固醇的膜结构域的组织作用。

Organization of a sterol-rich membrane domain by cdc15p during cytokinesis in fission yeast.

作者信息

Takeda Tetsuya, Kawate Toshimitsu, Chang Fred

机构信息

Department of Microbiology, Columbia University College of Physicians and Surgeons, 701 West 168th St, New York, NY 10032, USA.

出版信息

Nat Cell Biol. 2004 Nov;6(11):1142-4. doi: 10.1038/ncb1189. Epub 2004 Nov 1.

DOI:10.1038/ncb1189
PMID:15517003
Abstract

Many membrane processes occur in discrete membrane domains containing lipid rafts, 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 site. Here, we show that formation of this membrane domain is independent of the contractile actin ring, septation, mid1p and the septins, and also requires cdc15p, 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.

摘要

许多膜过程发生在含有脂筏的离散膜结构域中,但对于这些结构域是如何组织和定位的却知之甚少。在裂殖酵母粟酒裂殖酵母中,富含固醇的膜结构域在细胞分裂位点形成。在这里,我们表明这个膜结构域的形成独立于收缩性肌动蛋白环、隔膜形成、Mid1p和隔膜蛋白,并且还需要Cdc15p,一种与脂筏相关的必需收缩环蛋白。Cdc15突变体具有螺旋状的膜结构域。在间期细胞中过表达Cdc15p以肌动蛋白非依赖的方式诱导异常膜结构域的形成。我们提出Cdc15p的功能是在胞质分裂的切割位点组织脂筏。

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