1999 Fiscal Year Final Research Report Summary
Membrane phospholipid dynamics and cytoskeletal organization: Regulation of actin filament assembly by redistribution of membrane surface phospholipid
| Project/Area Number |
09480201
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Cell biology
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| Research Institution | Tokyo Metropolitan Organization for Medical Research |
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Principal Investigator |
UMEDA Masato The Tokyo Metropolitan Institute of Medical Science, Department of Molecular Biodynamics, 東京都臨床医学総合研究所, 研究員 (10185069)
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| Co-Investigator(Kenkyū-buntansha) |
TAKEUCHI Ken-ichi The Tokyo Metropolitan Institute of Medical Science, Department of Molecular Biodynamics, 東京都臨床医学総合研究所, 研究員 (70270684)
ITOH Kouichi The Tokyo Metropolitan Institute of Medical Science, Department of Molecular Biodynamics, 東京都臨床医学総合研究所, 研究員 (30291149)
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| Project Period (FY) |
1997 – 1999
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| Keywords | phospholipid / cytoskeleton / lipid bilayer / membrane / neuron / actin / yeast / phosphatidylethanolamine |
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| Research Abstract |
Using a novel peptide probe, Ro09-0198, which specifically forms a tight equimolar complex with phosphatidylethanoalmaine (PE) on biological membranes, we have analyzed the cell surface movement of PE in dividing CHO cells. We found that flip-flop of plasma membrane PE was markedly enhanced at the cleavage furrow during the late telophase of cytokinesis and that cell surface trapping of PE induced by adding the peptide-streptavidin complex to the mitotic cells blocked cytokinesis at the late telophase. Further analysis have shown that the redistribution of plasma membrane phospholipids acts as a regulator of actin filament assembly and play a crucial role in mediating a coordinate movement between plasma membrane and cytoskeleton. Molecules involved in the cross-talk between the phospholipid dynamics and cytoskeletal reorganization have been investigated using yeast and CHO mutant cells which were selected by their altered sensitivity to the PE-binding peptide.
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