Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission
AuthorsGromley, Adam Scott
Redick, Sambra D.
Doxsey, Stephen J.
Student AuthorsMinakshi Guha
UMass Chan AffiliationsProgram in Molecular Medicine
Document TypeJournal Article
KeywordsCell 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
Medicine and Health Sciences
MetadataShow full item record
AbstractThe 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.
SourceCell. 2005 Oct 7;123(1):75-87. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/33761
Related ResourcesLink to article in PubMed