4.8 Article

Removal of Stomatin,a Membrane-Associated Cell Division Protein, Results in Specific Cellular Lipid Changes

期刊

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 144, 期 39, 页码 18069-18074

出版社

AMER CHEMICAL SOC
DOI: 10.1021/jacs.2c07907

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资金

  1. European Research Council Consolidator Grant [306659]
  2. Wellcome Trust Investigator Award - K-CSC PhD Scholarship [110060/Z/15/Z.]
  3. Wellcome Trust [110060/Z/15/Z] Funding Source: Wellcome Trust
  4. European Research Council (ERC) [306659] Funding Source: European Research Council (ERC)

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The membrane protein stomatin is found to be involved in the cytokinesis step of cell division, even though it is not a lipid biosynthetic enzyme. Depletion of stomatin leads to changes in cellular lipidomes, and exogenous phosphatidylcholines can rescue these defects.
Lipids are key constituents of all cells, which express thousands of different lipid species. In most cases, it is not known why cells synthesize such diverse lipidomes, nor what regulates their metabolism. Although it is known that dividing cells specifically regulate their lipid content and that the correct lipid complement is required for successful division, it is unclear how lipids connect with the cell division machinery. Here, we report that the membrane protein stomatin is involved in the cytokinesis step of cell division. Although it is not a lipid biosynthetic enzyme, depletion of stomatin causes cells to change their lipidomes. These changes include specific lipid species, like ether lipids, and lipid families like phosphatidylcholines. Addition of exogenous phosphatidylcholines rescues stomatin-induced defects. These data suggest that stomatin interfaces with lipid metabolism. Stomatin has multiple contacts with the plasma membrane and we identify which sites are required for its role in cell division, as well as associated lipid shifts. We also show that stomatin's mobility on the plasma membrane changes during division, further supporting the requirement for a highly regulated physical interaction between membrane lipids and this newly identified cell division protein.

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