The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity

53BP1 is a key player in non-homologous end joining (NHEJ). Here the authors reveal an important role for the multifunctional homodimeric protein hub dynein light chain 1 (DYNLL1) in increasing the efficacy of 53BP1-mediated repair of DNA double-strand breaks (DSBs) by NHEJ.

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Autores principales:	Jordan R. Becker, Raquel Cuella-Martin, Marco Barazas, Rui Liu, Catarina Oliveira, Antony W. Oliver, Kirstin Bilham, Abbey B. Holt, Andrew N. Blackford, Jörg Heierhorst, Jos Jonkers, Sven Rottenberg, J. Ross Chapman
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c04551ad42a944b8b5da046f5825a9b4
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spelling	oai:doaj.org-article:c04551ad42a944b8b5da046f5825a9b42021-12-02T14:39:09ZThe ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity10.1038/s41467-018-07855-x2041-1723https://doaj.org/article/c04551ad42a944b8b5da046f5825a9b42018-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07855-xhttps://doaj.org/toc/2041-172353BP1 is a key player in non-homologous end joining (NHEJ). Here the authors reveal an important role for the multifunctional homodimeric protein hub dynein light chain 1 (DYNLL1) in increasing the efficacy of 53BP1-mediated repair of DNA double-strand breaks (DSBs) by NHEJ.Jordan R. BeckerRaquel Cuella-MartinMarco BarazasRui LiuCatarina OliveiraAntony W. OliverKirstin BilhamAbbey B. HoltAndrew N. BlackfordJörg HeierhorstJos JonkersSven RottenbergJ. Ross ChapmanNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jordan R. Becker Raquel Cuella-Martin Marco Barazas Rui Liu Catarina Oliveira Antony W. Oliver Kirstin Bilham Abbey B. Holt Andrew N. Blackford Jörg Heierhorst Jos Jonkers Sven Rottenberg J. Ross Chapman The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
description	53BP1 is a key player in non-homologous end joining (NHEJ). Here the authors reveal an important role for the multifunctional homodimeric protein hub dynein light chain 1 (DYNLL1) in increasing the efficacy of 53BP1-mediated repair of DNA double-strand breaks (DSBs) by NHEJ.
format	article
author	Jordan R. Becker Raquel Cuella-Martin Marco Barazas Rui Liu Catarina Oliveira Antony W. Oliver Kirstin Bilham Abbey B. Holt Andrew N. Blackford Jörg Heierhorst Jos Jonkers Sven Rottenberg J. Ross Chapman
author_facet	Jordan R. Becker Raquel Cuella-Martin Marco Barazas Rui Liu Catarina Oliveira Antony W. Oliver Kirstin Bilham Abbey B. Holt Andrew N. Blackford Jörg Heierhorst Jos Jonkers Sven Rottenberg J. Ross Chapman
author_sort	Jordan R. Becker
title	The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
title_short	The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
title_full	The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
title_fullStr	The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
title_full_unstemmed	The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity
title_sort	asciz-dynll1 axis promotes 53bp1-dependent non-homologous end joining and parp inhibitor sensitivity
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c04551ad42a944b8b5da046f5825a9b4
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The ASCIZ-DYNLL1 axis promotes 53BP1-dependent non-homologous end joining and PARP inhibitor sensitivity

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