Gromley, Adam ScottYeaman, CharlesRosa, JackRedick, Sambra D.Chen, Chun-TingMirabelle, StephanieGuha, MinakshiSillibourne, JamesDoxsey, Stephen J.2022-08-232022-08-232005-10-112008-09-17Cell. 2005 Oct 7;123(1):75-87. <a href="http://dx.doi.org/10.1016/j.cell.2005.07.027">Link to article on publisher's site</a>0092-8674 (Print)10.1016/j.cell.2005.07.02716213214https://hdl.handle.net/20.500.14038/33761The 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.en-USJournal Articlehttps://escholarship.umassmed.edu/gsbs_sp/421632031gsbs_sp/421