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    Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission

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    Authors
    Gromley, Adam Scott
    Yeaman, Charles
    Rosa, Jack
    Redick, Sambra D.
    Chen, Chun-Ting
    Mirabelle, Stephanie
    Guha, Minakshi
    Sillibourne, James
    Doxsey, Stephen J.
    Student Authors
    Minakshi Guha
    UMass Chan Affiliations
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    2005-10-11
    Keywords
    Cell Cycle Proteins; Cell Line, Transformed; Cytokinesis; Green Fluorescent Proteins; Humans; Macromolecular Substances; Membrane Fusion; Models, Molecular; Secretory Vesicles; Vesicular Transport Proteins
    Cell and Developmental Biology
    Life Sciences
    Medicine and Health Sciences
    
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    Link to Full Text
    http://dx.doi.org/10.1016/j.cell.2005.07.027
    Abstract
    The terminal step in cytokinesis, called abscission, requires resolution of the membrane connection between two prospective daughter cells. Our previous studies demonstrated that the coiled-coil protein centriolin localized to the midbody during cytokinesis and was required for abscission. Here we show that centriolin interacts with proteins of vesicle-targeting exocyst complexes and vesicle-fusion SNARE complexes. These complexes require centriolin for localization to a unique midbody-ring structure, and disruption of either complex inhibits abscission. Exocyst disruption induces accumulation of v-SNARE-containing vesicles at the midbody ring. In control cells, these v-SNARE vesicles colocalize with a GFP-tagged secreted polypeptide. The vesicles move to the midbody ring asymmetrically from one prospective daughter cell; the GFP signal is rapidly lost, suggesting membrane fusion; and subsequently the cell cleaves at the site of vesicle delivery/fusion. We propose that centriolin anchors protein complexes required for vesicle targeting and fusion and integrates membrane-vesicle fusion with abscission.
    Source
    Cell. 2005 Oct 7;123(1):75-87. Link to article on publisher's site
    DOI
    10.1016/j.cell.2005.07.027
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/33761
    PubMed ID
    16213214
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.cell.2005.07.027
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