Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis

Serine hydroxymethyltransferase 2 (SHMT2) converts serine to glycine in mitochondria and is upregulated in a variety of cancers. Here the authors show that acetylation of the lysine-95 (K95) residue negatively regulates SHMT2 expression and activity and is deacetylated by SIRT3 in colorectal cancer.

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Autores principales:	Zhen Wei, Jinglue Song, Guanghui Wang, Ximao Cui, Jun Zheng, Yunlan Tang, Xinyuan Chen, Jixi Li, Long Cui, Chen-Ying Liu, Wei Yu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5ca31543d90f4f24bd6dbf9f5eecaafa
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spelling	oai:doaj.org-article:5ca31543d90f4f24bd6dbf9f5eecaafa2021-12-02T15:34:36ZDeacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis10.1038/s41467-018-06812-y2041-1723https://doaj.org/article/5ca31543d90f4f24bd6dbf9f5eecaafa2018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06812-yhttps://doaj.org/toc/2041-1723Serine hydroxymethyltransferase 2 (SHMT2) converts serine to glycine in mitochondria and is upregulated in a variety of cancers. Here the authors show that acetylation of the lysine-95 (K95) residue negatively regulates SHMT2 expression and activity and is deacetylated by SIRT3 in colorectal cancer.Zhen WeiJinglue SongGuanghui WangXimao CuiJun ZhengYunlan TangXinyuan ChenJixi LiLong CuiChen-Ying LiuWei YuNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-16 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Zhen Wei Jinglue Song Guanghui Wang Ximao Cui Jun Zheng Yunlan Tang Xinyuan Chen Jixi Li Long Cui Chen-Ying Liu Wei Yu Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis
description	Serine hydroxymethyltransferase 2 (SHMT2) converts serine to glycine in mitochondria and is upregulated in a variety of cancers. Here the authors show that acetylation of the lysine-95 (K95) residue negatively regulates SHMT2 expression and activity and is deacetylated by SIRT3 in colorectal cancer.
format	article
author	Zhen Wei Jinglue Song Guanghui Wang Ximao Cui Jun Zheng Yunlan Tang Xinyuan Chen Jixi Li Long Cui Chen-Ying Liu Wei Yu
author_facet	Zhen Wei Jinglue Song Guanghui Wang Ximao Cui Jun Zheng Yunlan Tang Xinyuan Chen Jixi Li Long Cui Chen-Ying Liu Wei Yu
author_sort	Zhen Wei
title	Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis
title_short	Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis
title_full	Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis
title_fullStr	Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis
title_full_unstemmed	Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis
title_sort	deacetylation of serine hydroxymethyl-transferase 2 by sirt3 promotes colorectal carcinogenesis
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/5ca31543d90f4f24bd6dbf9f5eecaafa
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Deacetylation of serine hydroxymethyl-transferase 2 by SIRT3 promotes colorectal carcinogenesis

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