Function and molecular mechanism of N-terminal acetylation in autophagy

Summary: Acetyl ligation to the amino acids in a protein is an important posttranslational modification. However, in contrast to lysine acetylation, N-terminal acetylation is elusive in terms of its cellular functions. Here, we identify Nat3 as an N-terminal acetyltransferase essential for autophagy...

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Autores principales:	Tianyun Shen, Lan Jiang, Xinyuan Wang, Qingjia Xu, Lu Han, Shiyan Liu, Ting Huang, Hongyan Li, Lunzhi Dai, Huihui Li, Kefeng Lu
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/24ffbeca3fe74fd693bbb1b3f4b3f6ca
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spelling	oai:doaj.org-article:24ffbeca3fe74fd693bbb1b3f4b3f6ca2021-11-18T04:47:48ZFunction and molecular mechanism of N-terminal acetylation in autophagy2211-124710.1016/j.celrep.2021.109937https://doaj.org/article/24ffbeca3fe74fd693bbb1b3f4b3f6ca2021-11-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2211124721014108https://doaj.org/toc/2211-1247Summary: Acetyl ligation to the amino acids in a protein is an important posttranslational modification. However, in contrast to lysine acetylation, N-terminal acetylation is elusive in terms of its cellular functions. Here, we identify Nat3 as an N-terminal acetyltransferase essential for autophagy, a catabolic pathway for bulk transport and degradation of cytoplasmic components. We identify the actin cytoskeleton constituent Act1 and dynamin-like GTPase Vps1 (vacuolar protein sorting 1) as substrates for Nat3-mediated N-terminal acetylation of the first methionine. Acetylated Act1 forms actin filaments and therefore promotes the transport of Atg9 vesicles for autophagosome formation; acetylated Vps1 recruits and facilitates bundling of the SNARE (soluble N-ethylmaleimide-sensitive factor activating protein receptor) complex for autophagosome fusion with vacuoles. Abolishment of the N-terminal acetylation of Act1 and Vps1 is associated with blockage of upstream and downstream steps of the autophagy process. Therefore, our work shows that protein N-terminal acetylation plays a critical role in controlling autophagy by fine-tuning multiple steps in the process.Tianyun ShenLan JiangXinyuan WangQingjia XuLu HanShiyan LiuTing HuangHongyan LiLunzhi DaiHuihui LiKefeng LuElsevierarticleBiology (General)QH301-705.5ENCell Reports, Vol 37, Iss 7, Pp 109937- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Tianyun Shen Lan Jiang Xinyuan Wang Qingjia Xu Lu Han Shiyan Liu Ting Huang Hongyan Li Lunzhi Dai Huihui Li Kefeng Lu Function and molecular mechanism of N-terminal acetylation in autophagy
description	Summary: Acetyl ligation to the amino acids in a protein is an important posttranslational modification. However, in contrast to lysine acetylation, N-terminal acetylation is elusive in terms of its cellular functions. Here, we identify Nat3 as an N-terminal acetyltransferase essential for autophagy, a catabolic pathway for bulk transport and degradation of cytoplasmic components. We identify the actin cytoskeleton constituent Act1 and dynamin-like GTPase Vps1 (vacuolar protein sorting 1) as substrates for Nat3-mediated N-terminal acetylation of the first methionine. Acetylated Act1 forms actin filaments and therefore promotes the transport of Atg9 vesicles for autophagosome formation; acetylated Vps1 recruits and facilitates bundling of the SNARE (soluble N-ethylmaleimide-sensitive factor activating protein receptor) complex for autophagosome fusion with vacuoles. Abolishment of the N-terminal acetylation of Act1 and Vps1 is associated with blockage of upstream and downstream steps of the autophagy process. Therefore, our work shows that protein N-terminal acetylation plays a critical role in controlling autophagy by fine-tuning multiple steps in the process.
format	article
author	Tianyun Shen Lan Jiang Xinyuan Wang Qingjia Xu Lu Han Shiyan Liu Ting Huang Hongyan Li Lunzhi Dai Huihui Li Kefeng Lu
author_facet	Tianyun Shen Lan Jiang Xinyuan Wang Qingjia Xu Lu Han Shiyan Liu Ting Huang Hongyan Li Lunzhi Dai Huihui Li Kefeng Lu
author_sort	Tianyun Shen
title	Function and molecular mechanism of N-terminal acetylation in autophagy
title_short	Function and molecular mechanism of N-terminal acetylation in autophagy
title_full	Function and molecular mechanism of N-terminal acetylation in autophagy
title_fullStr	Function and molecular mechanism of N-terminal acetylation in autophagy
title_full_unstemmed	Function and molecular mechanism of N-terminal acetylation in autophagy
title_sort	function and molecular mechanism of n-terminal acetylation in autophagy
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/24ffbeca3fe74fd693bbb1b3f4b3f6ca
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Function and molecular mechanism of N-terminal acetylation in autophagy

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