Evidence map›Paper›PMID 26370501›Full record

ArticleThe Journal of cell biology2015

Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion.

Liming Yan, Sha Sun, Wei Wang, Juanming Shi, Xiaoyu Hu, Shiyan Wang, Dan Su, Zihe Rao, Junjie Hu, Zhiyong Lou

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. 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
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023
    Article
  10. The atlastin paralogs: The complexity in the tails.The Journal of cell biology · 2023
    Article
  11. Lipid and Lipidation in Membrane Fusion.The Journal of membrane biology · 2022
    Review
  12. Evolution of factors shaping the endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Atlastin-mediated membrane tethering is critical for cargo mobility and exit from the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

10 authors at 6 institutions in 1 country.

Liming YanSchool of Medicine, Tsinghua University, Beijing, China 100084.
Sha SunDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University and Tianjin Key Laboratory of Protein Sciences, Tianjin, China 300071.
Wei WangSchool of Medicine, Tsinghua University, Beijing, China 100084 State Key Laboratory of Cotton Biology, Key Laboratory of Plant Stress Biology, Henan University, Kaifeng, China 475004.
Juanming ShiDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University and Tianjin Key Laboratory of Protein Sciences, Tianjin, China 300071.
Xiaoyu HuDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University and Tianjin Key Laboratory of Protein Sciences, Tianjin, China 300071.
Shiyan WangState Key Laboratory of Cotton Biology, Key Laboratory of Plant Stress Biology, Henan University, Kaifeng, China 475004.
Dan SuCollaborative Innovation Center for Biotherapy, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, West China Medical School, Sichuan University, Chengdu, China 610041.
Zihe RaoSchool of Medicine, Tsinghua University, Beijing, China 100084 National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, China 100101 Collaborative Innovation Center for Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu, China 610041 huj@ibp.ac.cn louzy@mail.tsinghua.edu.cn.
Junjie HuDepartment of Genetics and Cell Biology, College of Life Sciences, Nankai University and Tianjin Key Laboratory of Protein Sciences, Tianjin, China 300071 National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing, China 100101 huj@ibp.ac.cn louzy@mail.tsinghua.edu.cn.
Zhiyong LouSchool of Medicine, Tsinghua University, Beijing, China 100084 Collaborative Innovation Center for Biotherapy, West China Hospital, West China Medical School, Sichuan University, Chengdu, China 610041.
Nankai University · CNWest China Medical Center of Sichuan University · CNHenan University · CNState Key Laboratory of BiotherapyState Key Laboratory of Cotton BiologyTsinghua University · CN

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Homotypic membrane fusion of the endoplasmic reticulum is mediated by dynamin-like guanosine triphosphatases (GTPases), which include atlastin (ATL) in metazoans and Sey1p in yeast. In this paper, we determined the crystal structures of the cytosolic domain of Sey1p derived from Candida albicans. The structures reveal a stalk-like, helical bundle domain following the GTPase, which represents a previously unidentified configuration of the dynamin superfamily. This domain is significantly longer than that of ATL and critical for fusion. Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AlF4(-) but is monomeric with GDP. Surprisingly, Sey1p could mediate fusion without GTP hydrolysis, even though fusion was much more efficient with GTP. Sey1p was able to replace ATL in mammalian cells, and the punctate localization of Sey1p was dependent on its GTPase activity. Despite the common function of fusogenic GTPases, our results reveal unique features of Sey1p.

Indexed as

Membrane FusionAnimalsApoptosis Inducing FactorCandida albicansChlorocebus aethiopsCOS CellsCrystallizationCrystallography, X-RayEndoplasmic ReticulumFungal ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateGuanylyl ImidodiphosphateHydrolysisModels, MolecularApoptosis Inducing FactorFungal ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateGuanylyl ImidodiphosphateSaccharomyces cerevisiae ProteinsSEY1 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID26370501
PMCPMC4576867
OpenAlexW2176389569

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.