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

Authors: Dukes, JD  Richardson, JD  Simmons, R  Whitley, P 
Citation: Dukes JD, etal., Biochem J. 2008 Apr 15;411(2):233-9.
Pubmed: (View Article at PubMed) PMID:18076377
DOI: Full-text: DOI:10.1042/BJ20071296

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 ESCRT (endosomal sorting complexes required for transport) that are normally involved in late endosome to lysosome trafficking have also been implicated in abscission. Here, we report that a subunit, CHMP3 (charged multivesicular body protein-3), of ESCRT-III localizes at the midbody. Deletion of the C-terminal autoinhibitory domain of CHMP3 inhibits cytokinesis. At the midbody, CHMP3 does not co-localize with Rab11, suggesting that it is not present on recycling endosomes. These results combined provide compelling evidence that proteins involved in late endosomal function are necessary for the end stages of cytokinesis.


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RGD Object Information
RGD ID: 4892661
Created: 2011-02-28
Species: All species
Last Modified: 2011-02-28
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.