Cited by 326Mitochondrial Function and PathologyAutophagy in Disease and TherapyProtein Structure and Dynamics

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MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

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Cao, Yu-Lu, Meng, Shuxia, Chen, Yang, Feng, Jian-Xiong, Gu, Dong-Dong, Yu, Bing, Li, Yu-Jie, Yang, Jin-Yu, Liao, Shuang, Chan, David C., Gao, Song·2017·Nature

DOI 10.1038/nature21077PMC PMC5319402

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Abstract

Mitochondria are double-membraned organelles with variable shapes influenced by metabolic conditions, developmental stage, and environmental stimuli. Their dynamic morphology is a result of regulated and balanced fusion and fission processes. Fusion is crucial for the health and physiological functions of mitochondria, including complementation of damaged mitochondrial DNAs and the maintenance of membrane potential. Mitofusins are dynamin-related GTPases that are essential for mitochondrial fusion. They are embedded in the mitochondrial outer membrane and thought to fuse adjacent mitochondria via combined oligomerization and GTP hydrolysis. However, the molecular mechanisms of this process remain unknown. Here we present crystal structures of engineered human MFN1 containing the GTPase domain and a helical domain during different stages of GTP hydrolysis. The helical domain is composed of elements from widely dispersed sequence regions of MFN1 and resembles the 'neck' of the bacterial dynamin-like protein. The structures reveal unique features of its catalytic machinery and explain how GTP binding induces conformational changes to promote GTPase domain dimerization in the transition state. Disruption of GTPase domain dimerization abolishes the fusogenic activity of MFN1. Moreover, a conserved aspartate residue trigger was found to affect mitochondrial elongation in MFN1, probably through a GTP-loading-dependent domain rearrangement. Thus, we propose a mechanistic model for MFN1-mediated mitochondrial tethering, and our results shed light on the molecular basis of mitochondrial fusion and mitofusin-related human neuromuscular disorders.

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A short history of SHELX
Sheldrick, G. M. (2007) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767307043930 · Cited by 88,113
CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
XDS
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MolProbity : all-atom structure validation for macromolecular crystallography
Chen, V. B., Arendall, W. B., Headd, J. J., Keedy, D. A., Immormino, R. M., Kapral, G. J., Murray, L. W., Richardson, J. S., & Richardson, D. C. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909042073 · Cited by 14,115

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Authors: Cao, Y.-L., Meng, S., Chen, Y., Feng, J.-X., Gu, D.-D., Yu, B., Li, Y.-J., Yang, J.-Y., Liao, S., Chan, D. C., & Gao, S.
Affiliations: Sun Yat-sen University (CN)
California Institute of Technology (US)
Corresponding author: Gao, Song
ORCID: Cao, Yu-Lu
Chen, Yang
Yu, Bing
Liao, Shuang
Chan, David C.
Gao, Song
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2017-01-23
Volume: 542
Issue: 7641
Pages: 372-376
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature21077
PMC: PMC5319402
OpenAlex: W2581248702
Cited by: 326
References: 53
Citations by year: 2026: 28 · 2025: 37 · 2024: 22 · 2023: 40 · 2022: 44 · 2021: 35 · 2020: 35 · 2019: 34 · 2018: 35 · 2017: 16
FWCI: 13.41
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
Funders: National Institute of General Medical Sciences (R01GM119388, R01GM083121, R01GM110039)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords: mitofusin 1, mitochondrial fusion, GTP hydrolysis, conformational change, dynamin-related GTPase, mitochondrial outer membrane, helical domain, mitochondrial elongation, mitochondrial tethering, neuromuscular disorders, crystal structure
MeSH terms: Protein Domains, Amino Acid Sequence, Guanosine Triphosphate, Humans, Hydrolysis, Membrane Fusion, Membrane Potentials, Mitochondria, Models, Molecular, Tryptophan, Crystallography, X-Ray, GTP Phosphohydrolases, Mitochondrial Membrane Transport Proteins, Mitochondrial Membranes, Biocatalysis, Protein Multimerization, Mitochondrial Dynamics

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MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion

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