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Ensa controls S-phase length by modulating Treslin levels

Abstract

The Greatwall/Ensa/PP2A-B55 pathway is essential for controlling mitotic substrate phosphorylation and mitotic entry. Here, we investigate the effect of the knockdown of the Gwl substrate, Ensa, in human cells. Unexpectedly, Ensa knockdown promotes a dramatic extension of S phase associated with a lowered density of replication forks. Notably, Ensa depletion results in a decrease of Treslin levels, a pivotal protein for the firing of replication origins. Accordingly, the extended S phase in Ensa-depleted cells is completely rescued by the overexpression of Treslin. Our data herein reveal a new mechanism by which normal cells regulate S-phase duration by controlling the ubiquitin-proteasome degradation of Treslin in a Gwl/Ensa-dependent pathway.The Greatwall/Ensa/PP2A-B55 pathway controls mitotic substrate phosphorylation and mitotic entry. Here the authors show that cells regulate S phase duration by controlling the ubiquitin-proteasome degradation of Treslin in a Gwl/Ensa-dependent pathway.

Type Journal
ISBN 2041-1723 (Electronic) 2041-1723 (Linking)
Authors Charrasse, S.; Gharbi-Ayachi, A.; Burgess, A.; Vera, J.; Hached, K.; Raynaud, P.; Schwob, E.; Lorca, T.; Castro, A.
Responsible Garvan Author Dr Andrew Burgess
Publisher Name Nature Communications
Published Date 2017-08-08 00:00:00
Published Volume 8
Published Issue 1
Published Pages 206
Status Published in-print
URL link to publisher's version https://www.ncbi.nlm.nih.gov/pubmed/28785014