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

Cell. 2005 Oct 7;123(1):75-87. doi: 10.1016/j.cell.2005.07.027.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cell Cycle Proteins / metabolism*
  • Cell Line, Transformed
  • Cytokinesis / physiology*
  • Green Fluorescent Proteins / metabolism
  • Humans
  • Macromolecular Substances / metabolism
  • Membrane Fusion / physiology
  • Models, Molecular
  • Secretory Vesicles / metabolism*
  • Vesicular Transport Proteins / metabolism


  • CNTRL protein, human
  • Cell Cycle Proteins
  • Macromolecular Substances
  • SNAPIN protein, human
  • Vesicular Transport Proteins
  • Green Fluorescent Proteins