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MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion
Open accessAbstract
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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“GTP hydrolysis of MFN1 causes a conformational change that allows the OMMs of opposing mitochondria to contact and fuse [61, 62].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [62]
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Metadata
- 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
- Venue
- Nature
- Published
- 2017-01-23
- Volume
- 542
- Issue
- 7641
- Pages
- 372-376
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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