The Cockayne syndrome group A and B proteins are part of a ubiquitin–proteasome degradation complex regulating cell division

Elena Paccosi, Federico Costanzo, Michele Costantino, Alessio Balzerano, Laura Monteonofrio, Silvia Soddu, Giorgio Prantera, Stefano Brancorsini, Jean Marc Egly, Luca Proietti-De-Santis

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)30498-30508
Number of pages11
JournalProceedings of the National Academy of Sciences of the United States of America
Volume117
Issue number48
DOIs
Publication statusPublished - Dec 1 2020

Keywords

  • Cockayne syndrome | cytokinesis | cell division | abscission | ubiquitination

ASJC Scopus subject areas

  • General

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