Evidence map›Paper›PMID 29093165›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Sequences flanking the transmembrane segments facilitate mitochondrial localization and membrane fusion by mitofusin.

Xiaofang Huang, Xin Zhou, Xiaoyu Hu, Amit S Joshi, Xiangyang Guo, Yushan Zhu, Quan Chen, William A Prinz, Junjie Hu

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. PMF proteins mediate mitochondrial fusion in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Mitochondrial Surveillance by Cdc48/p97: MAD vs. Membrane Fusion.International journal of molecular sciences · 2020
    Review
  17. Article
  18. Review
  19. Article
  20. Structural analysis of a trimeric assembly of the mitochondrial dynamin-like GTPase Mgm1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Xiaofang HuangDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
Xin ZhouDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
Xiaoyu HuDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
Amit S JoshiLaboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Xiangyang GuoDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
Yushan ZhuDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
Quan ChenDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China.
William A PrinzLaboratory of Cell and Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.
Junjie HuDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University, Tianjin 300071, China; huj@ibp.ac.cn.ORCID 0000-0003-4712-2243
Nankai University · CNNational Institutes of Health · USChinese Academy of Sciences · CN

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Mitochondria constantly divide and fuse. Homotypic fusion of the outer mitochondrial membranes requires the mitofusin (MFN) proteins, a family of dynamin-like GTPases. MFNs are anchored in the membrane by transmembrane (TM) segments, exposing both the N-terminal GTPase domain and the C-terminal tail (CT) to the cytosol. This arrangement is very similar to that of the atlastin (ATL) GTPases, which mediate fusion of endoplasmic reticulum (ER) membranes. We engineered various MFN-ATL chimeras to gain mechanistic insight into MFN-mediated fusion. When MFN1 is localized to the ER by TM swapping with ATL1, it functions in the maintenance of ER morphology and fusion. In addition, an amphipathic helix in the CT of MFN1 is exchangeable with that of ATL1 and critical for mitochondrial localization of MFN1. Furthermore, hydrophobic residues N-terminal to the TM segments of MFN1 play a role in membrane targeting but not fusion. Our findings provide important insight into MFN-mediated membrane fusion.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsEndoplasmic ReticulumGTP-Binding ProteinsGTP PhosphohydrolasesMembrane FusionMembrane ProteinsMicroscopy, FluorescenceMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsModels, MolecularProtein ConformationSequence AlignmentYeastsATL1 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesMembrane ProteinsMitochondrial Membrane Transport Proteinsendoplasmic reticulummembrane fusionmembrane targetingmitochondriamitofusin

Identifiers

PMID29093165
PMCPMC5699052
OpenAlexW2767117834

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.