Please use this identifier to cite or link to this item: http://hdl.handle.net/2067/42476
Title: The Cockayne syndrome group A and B proteins are part of a ubiquitin-proteasome degradation complex regulating cell division
Authors: Paccosi, Elena
Costanzo, Federico
Costantino, Michele
Balzerano, Alessio
Monteonofrio, Laura
Soddu, Silvia
Prantera, Giorgio 
Brancorsini, Stefano
Egly, Jean-Marc
Proietti De Santis, Luca 
Journal: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 
Issue Date: 2020
Abstract: 
Cytokinesis is monitored by a molecular machinery that promotes the degradation of the intercellular bridge, a transient protein structure connecting the two daughter cells. Here, we found that CSA and CSB, primarily defined as DNA repair factors, are located at the midbody, a transient structure in the middle of the intercellular bridge, where they recruit CUL4 and MDM2 ubiquitin ligases and the proteasome. As a part of this molecular machinery, CSA and CSB contribute to the ubiquitination and the degradation of proteins such as PRC1, the Protein Regulator of Cytokinesis, to ensure the correct separation of the two daughter cells. Defects in CSA or CSB result in perturbation of the abscission leading to the formation of long intercellular bridges and multinucleated cells, which might explain part of the Cockayne syndrome phenotypes. Our results enlighten the role played by CSA and CSB as part of a ubiquitin/proteasome degradation process involved in transcription, DNA repair, and cell division.
URI: http://hdl.handle.net/2067/42476
ISSN: 0027-8424
DOI: 10.1073/pnas.2006543117
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