A dominant negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes

Joseph D Dukes , Judith D Richardson , Ruth Simmons , Paul Whitley (1)

1 Department of Biology and Biochemistry

In eukaryotic cells, the completion of cytokinesis is dependent on membrane trafficking events to deliver membrane to the site of abscission. Golgi and recycling endosomal derived proteins are required for the terminal stages of cytokinesis. Recently, protein subunits of the Endosomal Sorting Complex Required for Transport (ESCRT) that are normally involved in late endosome to lysosome trafficking have also been implicated in abscission. Here we report that a subunit, Charged Multivesicular Body Protein-3 (CHMP3), of ESCRT-III localises at the midbody. Deletion of the C-terminal autoinhibitory domain of CHMP3 inhibits cytokinesis. At the midbody, CHMP3 does not co-localise with Rab11 suggesting that it is not present on recycling endosomes. These data combined provide compelling evidence that proteins involved in late endosomal function are necessary for the end stages of cytokinesis.

Mots clés: Life Sciences

Joseph D Dukes, Judith D Richardson, Ruth Simmons, Paul Whitley. A dominant negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes. Biochemical Journal, 2008, 411 (2), pp.233-239. ⟨10.1042/BJ20071296⟩. ⟨hal-00478885⟩