Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1

Incessant telomere synthesis in cancer cells depends on specific mutations in the TERT promoter, enabling its activation by transcription factors ETS1 and p52. Here, the authors elucidate the structural basis for p52/ETS1 binding to mutant TERT, suggesting a general mechanism for TERT reactivation i...

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Autores principales:	Xueyong Xu, Yinghui Li, Sakshibeedu R. Bharath, Mert Burak Ozturk, Matthew W. Bowler, Bryan Zong Lin Loo, Vinay Tergaonkar, Haiwei Song
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/26d841da334f432d89039230bd2c2068
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spelling	oai:doaj.org-article:26d841da334f432d89039230bd2c20682021-12-02T15:34:19ZStructural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS110.1038/s41467-018-05644-02041-1723https://doaj.org/article/26d841da334f432d89039230bd2c20682018-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-05644-0https://doaj.org/toc/2041-1723Incessant telomere synthesis in cancer cells depends on specific mutations in the TERT promoter, enabling its activation by transcription factors ETS1 and p52. Here, the authors elucidate the structural basis for p52/ETS1 binding to mutant TERT, suggesting a general mechanism for TERT reactivation in cancer.Xueyong XuYinghui LiSakshibeedu R. BharathMert Burak OzturkMatthew W. BowlerBryan Zong Lin LooVinay TergaonkarHaiwei SongNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Xueyong Xu Yinghui Li Sakshibeedu R. Bharath Mert Burak Ozturk Matthew W. Bowler Bryan Zong Lin Loo Vinay Tergaonkar Haiwei Song Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
description	Incessant telomere synthesis in cancer cells depends on specific mutations in the TERT promoter, enabling its activation by transcription factors ETS1 and p52. Here, the authors elucidate the structural basis for p52/ETS1 binding to mutant TERT, suggesting a general mechanism for TERT reactivation in cancer.
format	article
author	Xueyong Xu Yinghui Li Sakshibeedu R. Bharath Mert Burak Ozturk Matthew W. Bowler Bryan Zong Lin Loo Vinay Tergaonkar Haiwei Song
author_facet	Xueyong Xu Yinghui Li Sakshibeedu R. Bharath Mert Burak Ozturk Matthew W. Bowler Bryan Zong Lin Loo Vinay Tergaonkar Haiwei Song
author_sort	Xueyong Xu
title	Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_short	Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_full	Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_fullStr	Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_full_unstemmed	Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1
title_sort	structural basis for reactivating the mutant tert promoter by cooperative binding of p52 and ets1
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/26d841da334f432d89039230bd2c2068
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_version_	1718386887832371200

Structural basis for reactivating the mutant TERT promoter by cooperative binding of p52 and ETS1

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