A novel human protein of the maternal centriole is required for the final stages of cytokinesis and entry into S phase
AuthorsGromley, Adam Scott
Mogensen, Mette M.
Doxsey, Stephen J.
KeywordsAmino Acid Sequence; Animals; Antibodies; Base Sequence; COS Cells; Cell Cycle Proteins; Cell Division; Centrioles; Cytoskeletal Proteins; DNA, Complementary; Deoxyribonucleases; Embryo, Nonmammalian; Eukaryotic Cells; Hela Cells; Humans; Immunohistochemistry; Microscopy, Electron; Microtubules; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; RNA, Small Interfering; S Phase; Saccharomyces cerevisiae Proteins
Medicine and Health Sciences
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AbstractCentrosomes nucleate microtubules and contribute to mitotic spindle organization and function. They also participate in cytokinesis and cell cycle progression in ways that are poorly understood. Here we describe a novel human protein called centriolin that localizes to the maternal centriole and functions in both cytokinesis and cell cycle progression. Centriolin silencing induces cytokinesis failure by a novel mechanism whereby cells remain interconnected by long intercellular bridges. Most cells continue to cycle, reenter mitosis, and form multicellular syncytia. Some ultimately divide or undergo apoptosis specifically during the protracted period of cytokinesis. At later times, viable cells arrest in G1/G0. The cytokinesis activity is localized to a centriolin domain that shares homology with Nud1p and Cdc11p, budding and fission yeast proteins that anchor regulatory pathways involved in progression through the late stages of mitosis. The Nud1p-like domain of centriolin binds Bub2p, another component of the budding yeast pathway. We conclude that centriolin is required for a late stage of vertebrate cytokinesis, perhaps the final cell cleavage event, and plays a role in progression into S phase.
SourceJ Cell Biol. 2003 May 12;161(3):535-45. Epub 2003 May 5. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/33760
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