Damaged replication forks tolerate USP7 to maintain genome stability

Anastasia Zlatanou; Grant S. Stewart

doi:10.1080/23723556.2015.1063571

Damaged replication forks tolerate USP7 to maintain genome stability

Anastasia Zlatanou, Grant S. Stewart^*

^*Corresponding author for this work

Cancer and Genomic Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

RAD18 functions to promote DNA damage tolerance (DTT), a process that ensures faithful genome duplication. Protein ubiquitylation/deubiquitylation is a critical regulatory mechanism controlling DTT. Recently, we have identified the deubiquitylating enzyme USP7 as a component of the DTT machinery that acts to protect RAD18 from proteasome-dependent degradation.

Original language	English
Article number	e1063571
Journal	Molecular and Cellular Oncology
Volume	3
Issue number	1
DOIs	https://doi.org/10.1080/23723556.2015.1063571
Publication status	Published - 2 Jan 2016

Bibliographical note

Publisher Copyright:
© 2016, © 2016 Taylor & Francis Group, LLC.

ASJC Scopus subject areas

Molecular Medicine
Cancer Research

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1080/23723556.2015.1063571

Cite this

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abstract = "RAD18 functions to promote DNA damage tolerance (DTT), a process that ensures faithful genome duplication. Protein ubiquitylation/deubiquitylation is a critical regulatory mechanism controlling DTT. Recently, we have identified the deubiquitylating enzyme USP7 as a component of the DTT machinery that acts to protect RAD18 from proteasome-dependent degradation.",

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Damaged replication forks tolerate USP7 to maintain genome stability

Abstract

Bibliographical note

ASJC Scopus subject areas

UN SDGs

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