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"Lights, camera, (ac)tion!": Damage-induced PCBP1 deacetylation releases PARP1 to engage DNA double-strand breaks
Laura R Purkey1, Kyle M Miller1
1Department of Radiation Oncology, Winship Cancer Center, Emory University School of Medicine, Atlanta, GA 30322, USA.
Abstract:
In this issue, Shu et al.1 identify the RNA-binding protein PCBP1 as a PARP1 interactor and negative regulator, a function relieved by SIRT7 deacetylation of PCBP1 upon DNA damage. Tumor studies indicated clinical relevance of this pathway, especially in response to radiotherapy, in modulating PARP1 activity as a therapeutic strategy.
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