Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins

The deacetylase Sirt1, known to regulate many cellular functions, can be activated by energy deprivation, however the mechanism is unclear. Here, the authors show that ATP inhibits Sirt1 by binding to the C-terminal domain, and energy deprivation derepresses Sirt1 activity by lowering the ATP level.

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Autores principales:	Hyeog Kang, Shinichi Oka, Duck-Yeon Lee, Junhong Park, Angel M. Aponte, Young-Sang Jung, Jacob Bitterman, Peiyong Zhai, Yi He, Hamed Kooshapur, Rodolfo Ghirlando, Nico Tjandra, Sean B. Lee, Myung K. Kim, Junichi Sadoshima, Jay H. Chung
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b6335290698541848579c1e330cc3914
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spelling	oai:doaj.org-article:b6335290698541848579c1e330cc39142021-12-02T15:38:57ZSirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins10.1038/ncomms155602041-1723https://doaj.org/article/b6335290698541848579c1e330cc39142017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15560https://doaj.org/toc/2041-1723The deacetylase Sirt1, known to regulate many cellular functions, can be activated by energy deprivation, however the mechanism is unclear. Here, the authors show that ATP inhibits Sirt1 by binding to the C-terminal domain, and energy deprivation derepresses Sirt1 activity by lowering the ATP level.Hyeog KangShinichi OkaDuck-Yeon LeeJunhong ParkAngel M. AponteYoung-Sang JungJacob BittermanPeiyong ZhaiYi HeHamed KooshapurRodolfo GhirlandoNico TjandraSean B. LeeMyung K. KimJunichi SadoshimaJay H. ChungNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Hyeog Kang Shinichi Oka Duck-Yeon Lee Junhong Park Angel M. Aponte Young-Sang Jung Jacob Bitterman Peiyong Zhai Yi He Hamed Kooshapur Rodolfo Ghirlando Nico Tjandra Sean B. Lee Myung K. Kim Junichi Sadoshima Jay H. Chung Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
description	The deacetylase Sirt1, known to regulate many cellular functions, can be activated by energy deprivation, however the mechanism is unclear. Here, the authors show that ATP inhibits Sirt1 by binding to the C-terminal domain, and energy deprivation derepresses Sirt1 activity by lowering the ATP level.
format	article
author	Hyeog Kang Shinichi Oka Duck-Yeon Lee Junhong Park Angel M. Aponte Young-Sang Jung Jacob Bitterman Peiyong Zhai Yi He Hamed Kooshapur Rodolfo Ghirlando Nico Tjandra Sean B. Lee Myung K. Kim Junichi Sadoshima Jay H. Chung
author_facet	Hyeog Kang Shinichi Oka Duck-Yeon Lee Junhong Park Angel M. Aponte Young-Sang Jung Jacob Bitterman Peiyong Zhai Yi He Hamed Kooshapur Rodolfo Ghirlando Nico Tjandra Sean B. Lee Myung K. Kim Junichi Sadoshima Jay H. Chung
author_sort	Hyeog Kang
title	Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
title_short	Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
title_full	Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
title_fullStr	Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
title_full_unstemmed	Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins
title_sort	sirt1 carboxyl-domain is an atp-repressible domain that is transferrable to other proteins
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/b6335290698541848579c1e330cc3914
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Sirt1 carboxyl-domain is an ATP-repressible domain that is transferrable to other proteins

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