Sterol-rich plasma membrane domains in the fission yeast Schizosaccharomyces pombe.

Sterol-rich membrane domains exist in unicellular and multicellular eukaryotes. They are thought to provide a structural framework for interactions among a subset of proteins by selectively incorporating some proteins while excluding others. Although most studies have focused on the biophysical and biochemical properties of sterol-rich membrane domains and incorporated proteins, relatively little is known about their intracellular distribution. Using a cytological approach we show here that in the fission yeast Schizosaccharomyces pombe, sterols are enriched in the plasma membrane at the growing cell tips and at the site of cytokinesis. The distribution of sterols is regulated in a cell-cycle-dependent manner and requires a functional secretory pathway. By manipulating the integrity of sterol-rich membrane domains using sterol sequestering agents and genetic means, we show that these domains are important for multiple processes regulating cytokinesis. In these cells, defects in proper maintenance of the actomyosin ring and/or its attachment to the overlying plasma membrane were observed. Furthermore, the stability of a plasma membrane protein that colocalises with sterol-rich membrane domains was compromised. Taken together, our studies establish S. pombe as a genetically tractable model organism in which to study the role(s) of sterol-rich membrane domains in cell polarity and cytokinesis.