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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Autores principales: 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
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Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea: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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