A dominant-negative ESCRT-III protein perturbs cytokinesis and trafficking to lysosomes.
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.
Dukes
Joseph D
JD
Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, U.K.
Richardson
Judith D
JD
Simmons
Ruth
R
Whitley
Paul
P
D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D048749:Cytokinesis; D015870:Gene Expression; D006801:Humans; D008247:Lysosomes / Q000378:metabolism*; D009154:Mutation / Q000235:genetics; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism*; D021381:Protein Transport; D051381:Rats; D033921:Vesicular Transport Proteins / Q000378:metabolism*
D009687:Nuclear Proteins; D033921:Vesicular Transport Proteins