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dc.contributor.authorGromley, Adam Scott
dc.contributor.authorYeaman, Charles
dc.contributor.authorRosa, Jack
dc.contributor.authorRedick, Sambra D.
dc.contributor.authorChen, Chun-Ting
dc.contributor.authorMirabelle, Stephanie
dc.contributor.authorGuha, Minakshi
dc.contributor.authorSillibourne, James
dc.contributor.authorDoxsey, Stephen J.
dc.date2022-08-11T08:08:58.000
dc.date.accessioned2022-08-23T16:14:01Z
dc.date.available2022-08-23T16:14:01Z
dc.date.issued2005-10-11
dc.date.submitted2008-09-17
dc.identifier.citationCell. 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>
dc.identifier.issn0092-8674 (Print)
dc.identifier.doi10.1016/j.cell.2005.07.027
dc.identifier.pmid16213214
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33761
dc.description.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.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16213214&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/j.cell.2005.07.027
dc.subjectCell Cycle Proteins; Cell Line, Transformed; Cytokinesis; Green Fluorescent Proteins; Humans; Macromolecular Substances; Membrane Fusion; Models, Molecular; Secretory Vesicles; Vesicular Transport Proteins
dc.subjectCell and Developmental Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleCentriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission
dc.typeJournal Article
dc.source.journaltitleCell
dc.source.volume123
dc.source.issue1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/421
dc.identifier.contextkey632031
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/421
dc.contributor.departmentProgram in Molecular Medicine
dc.source.pages75-87
dc.contributor.studentMinakshi Guha


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