MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

Yu-Lu Cao, Shuxia Meng, Yang Chen, Jian-Xiong Feng, Dong-Dong Gu, Bing Yu, Yu-Jie Li, Jin-Yu Yang, Shuang Liao, David C. Chan and Song Gao ()
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Yu-Lu Cao: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Shuxia Meng: California Institute of Technology
Yang Chen: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Jian-Xiong Feng: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Dong-Dong Gu: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Bing Yu: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Yu-Jie Li: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Jin-Yu Yang: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
Shuang Liao: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center
David C. Chan: California Institute of Technology
Song Gao: State Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center

Nature, 2017, vol. 542, issue 7641, 372-376

Abstract: Crystal structures of engineered human MFN1 in different stages of GTP hydrolysis provide insights into the GTP-induced conformational changes that promote MFN1 dimerization to bring about mitochondrial fusion.

Date: 2017
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DOI: 10.1038/nature21077

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