You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Redistribution of Phosphatidylethanolamine at the Cleavage Furrow of Dividing Cells during Cytokinesis
Kazuo Emoto, Toshihide Kobayashi, Akiko Yamaji, Hiroyuki Aizawa, Ichiro Yahara, Keizo Inoue and Masato Umeda
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 23 (Nov. 12, 1996), pp. 12867-12872
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/40713
Page Count: 6
You can always find the topics here!Topics: Cell membranes, Erythrocytes, Cytokinesis, Daughter cells, Telophase, P branes, Delta cells, Biochemistry, Cell division, Liposomes
Were these topics helpful?See somethings inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
Ro09-0198 is a tetracyclic polypeptide of 19 amino acids that recognizes strictly the structure of phosphatidylethanolamine (PE) and forms a tight equimolar complex with PE on biological membranes. Using the cyclic peptide coupled with fluorescence-labeled streptavidin, we have analyzed the cell surface localization of PE in dividing Chinese hamster ovary cells. We found that PE was exposed on the cell surface specifically at the cleavage furrow during the late telophase of cytokinesis. PE was exposed on the cell surface only during the late telophase and no alteration in the distribution of the plasma membrane-bound cyclic peptide was observed during the cytokinesis, suggesting that the surface exposure of PE reflects the enhanced scrambling of PE at the cleavage furrow. Furthermore, cell surface immobilization of PE induced by adding the cyclic peptide coupled with streptavidin to prometaphase cells effectively blocked the cytokinesis at late telophase. The peptide-streptavidin complex treatment had no effect on furrowing, rearrangement of microtubules, and nuclear reconstitution, but specifically inhibited both actin filament disassembly at the cleavage furrow and subsequent membrane fusion. These results suggest that the redistribution of the plasma membrane phospholipids is a crucial step for cytokinesis and the cell surface PE may play a pivotal role in mediating a coordinate movement between the contractile ring and plasma membrane to achieve successful cell division.
Proceedings of the National Academy of Sciences of the United States of America © 1996 National Academy of Sciences