The Cockayne syndrome group A and B proteins are part of a ubiquitin-proteasome degradation complex regulating cell division.
Fiche publication
Date publication
novembre 2020
Journal
Proceedings of the National Academy of Sciences of the United States of America
Auteurs
Membres identifiés du Cancéropôle Est :
Dr EGLY Jean-Marc
Tous les auteurs :
Paccosi E, Costanzo F, Costantino M, Balzerano A, Monteonofrio L, Soddu S, Prantera G, Brancorsini S, Egly JM, Proietti-De-Santis L
Lien Pubmed
Résumé
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.
Mots clés
Cockayne syndrome, abscission, cell division, cytokinesis, ubiquitination
Référence
Proc Natl Acad Sci U S A. 2020 Nov 16;: