Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset

Mitofusin-2 (MFN2) is a dynamin-like GTPase that plays a central role in regulating mitochondrial fusion and cell metabolism. Here, authors report crystal structures of truncated human MFN2 in different nucleotide-loading states and show that MFN2 forms sustained dimers even after GTP hydrolysis.

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Auteurs principaux:	Yu-Jie Li, Yu-Lu Cao, Jian-Xiong Feng, Yuanbo Qi, Shuxia Meng, Jie-Feng Yang, Ya-Ting Zhong, Sisi Kang, Xiaoxue Chen, Lan Lan, Li Luo, Bing Yu, Shoudeng Chen, David C. Chan, Junjie Hu, Song Gao
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2019
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/20184dcb3f0a4e0db34a9f78850e0d8f
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spelling	oai:doaj.org-article:20184dcb3f0a4e0db34a9f78850e0d8f2021-12-02T16:57:11ZStructural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset10.1038/s41467-019-12912-02041-1723https://doaj.org/article/20184dcb3f0a4e0db34a9f78850e0d8f2019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12912-0https://doaj.org/toc/2041-1723Mitofusin-2 (MFN2) is a dynamin-like GTPase that plays a central role in regulating mitochondrial fusion and cell metabolism. Here, authors report crystal structures of truncated human MFN2 in different nucleotide-loading states and show that MFN2 forms sustained dimers even after GTP hydrolysis.Yu-Jie LiYu-Lu CaoJian-Xiong FengYuanbo QiShuxia MengJie-Feng YangYa-Ting ZhongSisi KangXiaoxue ChenLan LanLi LuoBing YuShoudeng ChenDavid C. ChanJunjie HuSong GaoNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yu-Jie Li Yu-Lu Cao Jian-Xiong Feng Yuanbo Qi Shuxia Meng Jie-Feng Yang Ya-Ting Zhong Sisi Kang Xiaoxue Chen Lan Lan Li Luo Bing Yu Shoudeng Chen David C. Chan Junjie Hu Song Gao Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
description	Mitofusin-2 (MFN2) is a dynamin-like GTPase that plays a central role in regulating mitochondrial fusion and cell metabolism. Here, authors report crystal structures of truncated human MFN2 in different nucleotide-loading states and show that MFN2 forms sustained dimers even after GTP hydrolysis.
format	article
author	Yu-Jie Li Yu-Lu Cao Jian-Xiong Feng Yuanbo Qi Shuxia Meng Jie-Feng Yang Ya-Ting Zhong Sisi Kang Xiaoxue Chen Lan Lan Li Luo Bing Yu Shoudeng Chen David C. Chan Junjie Hu Song Gao
author_facet	Yu-Jie Li Yu-Lu Cao Jian-Xiong Feng Yuanbo Qi Shuxia Meng Jie-Feng Yang Ya-Ting Zhong Sisi Kang Xiaoxue Chen Lan Lan Li Luo Bing Yu Shoudeng Chen David C. Chan Junjie Hu Song Gao
author_sort	Yu-Jie Li
title	Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
title_short	Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
title_full	Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
title_fullStr	Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
title_full_unstemmed	Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset
title_sort	structural insights of human mitofusin-2 into mitochondrial fusion and cmt2a onset
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/20184dcb3f0a4e0db34a9f78850e0d8f
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Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset

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