SAMHD1 sheds moonlight on DNA double-strand break repair.

Cabello-Lobato, Maria J; Wang, Siyue; Schmidt, Christine K

dc.contributor.author	Cabello-Lobato, Maria J
dc.contributor.author	Wang, Siyue
dc.contributor.author	Schmidt, Christine K
dc.date.accessioned	2017-10-19T20:32:23Z
dc.date.available	2017-10-19T20:32:23Z
dc.date.issued	2017-09-29
dc.identifier.citation	SAMHD1 sheds moonlight on DNA double-strand break repair. 2017, Trends Genet.	en
dc.identifier.issn	0168-9525
dc.identifier.pmid	28969870
dc.identifier.doi	10.1016/j.tig.2017.09.007
dc.identifier.uri	http://hdl.handle.net/10541/620603
dc.description.abstract	SAMHD1 (sterile α motif and histidine (H) aspartate (D) domain-containing protein 1) is known for its antiviral activity of hydrolysing deoxynucleotides required for virus replication. Daddacha et al. identify a hydrolase-independent, moonlighting function of SAMHD1 that facilitates homologous recombination of DNA double-strand breaks (DSBs) by promoting recruitment of C-terminal binding protein interacting protein (CTIP), a DNA-end resection factor, to damaged DNA. These findings could benefit anticancer treatment.
dc.language.iso	en	en
dc.rights	Archived with thanks to Trends in genetics : TIG	en
dc.title	SAMHD1 sheds moonlight on DNA double-strand break repair.	en
dc.type	Article	en
dc.contributor.department	Division of Cancer Sciences, School of Medical Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Cancer Research Centre Building, 555 Wilmslow Road, Manchester	en
dc.identifier.journal	Trends in Genetics : TIG	en
refterms.dateFOA	2018-12-17T15:04:49Z
html.description.abstract	SAMHD1 (sterile α motif and histidine (H) aspartate (D) domain-containing protein 1) is known for its antiviral activity of hydrolysing deoxynucleotides required for virus replication. Daddacha et al. identify a hydrolase-independent, moonlighting function of SAMHD1 that facilitates homologous recombination of DNA double-strand breaks (DSBs) by promoting recruitment of C-terminal binding protein interacting protein (CTIP), a DNA-end resection factor, to damaged DNA. These findings could benefit anticancer treatment.