Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics

AMPK is regulates cellular energy and has been extensively studied, although our knowledge of downstream substrates is incomplete. Here, Chen et al. perform global quantitative analysis for AMPK-dependent sites and validate one hit, ARMC10, as a direct AMPK effector of mitochondrial dynamics.

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Autores principales:	Zhen Chen, Caoqi Lei, Chao Wang, Nan Li, Mrinal Srivastava, Mengfan Tang, Huimin Zhang, Jong Min Choi, Sung Yun Jung, Jun Qin, Junjie Chen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c4d35187bada4634b09ee0cf3c4b49b5
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spelling	oai:doaj.org-article:c4d35187bada4634b09ee0cf3c4b49b52021-12-02T17:01:29ZGlobal phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics10.1038/s41467-018-08004-02041-1723https://doaj.org/article/c4d35187bada4634b09ee0cf3c4b49b52019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-08004-0https://doaj.org/toc/2041-1723AMPK is regulates cellular energy and has been extensively studied, although our knowledge of downstream substrates is incomplete. Here, Chen et al. perform global quantitative analysis for AMPK-dependent sites and validate one hit, ARMC10, as a direct AMPK effector of mitochondrial dynamics.Zhen ChenCaoqi LeiChao WangNan LiMrinal SrivastavaMengfan TangHuimin ZhangJong Min ChoiSung Yun JungJun QinJunjie ChenNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Zhen Chen Caoqi Lei Chao Wang Nan Li Mrinal Srivastava Mengfan Tang Huimin Zhang Jong Min Choi Sung Yun Jung Jun Qin Junjie Chen Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
description	AMPK is regulates cellular energy and has been extensively studied, although our knowledge of downstream substrates is incomplete. Here, Chen et al. perform global quantitative analysis for AMPK-dependent sites and validate one hit, ARMC10, as a direct AMPK effector of mitochondrial dynamics.
format	article
author	Zhen Chen Caoqi Lei Chao Wang Nan Li Mrinal Srivastava Mengfan Tang Huimin Zhang Jong Min Choi Sung Yun Jung Jun Qin Junjie Chen
author_facet	Zhen Chen Caoqi Lei Chao Wang Nan Li Mrinal Srivastava Mengfan Tang Huimin Zhang Jong Min Choi Sung Yun Jung Jun Qin Junjie Chen
author_sort	Zhen Chen
title	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
title_short	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
title_full	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
title_fullStr	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
title_full_unstemmed	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
title_sort	global phosphoproteomic analysis reveals armc10 as an ampk substrate that regulates mitochondrial dynamics
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/c4d35187bada4634b09ee0cf3c4b49b5
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Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics

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