Geylani's paper is out!

Congratulations to Geylani and team for publishing their work on how a CDK1 phospho-switch reprograms TRAIP to unload replisomes in mitosis. Geylani Can et al. show that a phospho-regulated architectural switch alters replisome organization in mitosis to safeguard genome integrity before chromosome segregation. During interphase, the replisome-associated E3 ubiquitin ligase TRAIP ubiquitylates barriers in front of the fork to allow replisome progression. In mitosis, TRAIP is reprogrammed from a trans-acting to a cis-acting ligase that can ubiquitylate the replisome itself. This enables the processing of unreplicated DNA, which can cause catastrophic chromosome segregation failure. This work describes the mechanism underlying TRAIP reprogramming: the ATPase TTF2 is recruited to the replisome, where its noncatalytic N-terminal domain tethers Cyclin B-CDK1-phosphorylated TRAIP to the leading strand DNA polymerase ε in a geometry that allows replisome ubiquitylation. Read the full story here!