Evidence map›Paper›PMID 22508509›Full record

ArticleThe Journal of cell biology2012

The dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiae.

Kamran Anwar, Robin W Klemm, Amanda Condon, Katharina N Severin, Miao Zhang, Rodolfo Ghirlando, Junjie Hu, Tom A Rapoport, William A Prinz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

82 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
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  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
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  11. Article
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  14. Review
  15. Article
  16. Article
  17. Evolution of factors shaping the endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2022
    Article
  18. A role for endoplasmic reticulum dynamics in the cellular distribution of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  19. Article
  20. Article

22 more citing papers are in PubMed but not listed here.

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 4 institutions in 3 countries.

Kamran AnwarLaboratory of Molecular and Cell Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.
Robin W Klemm
Amanda Condon
Katharina N Severin
Miao Zhang
Rodolfo Ghirlando
Junjie Hu
Tom A Rapoport
William A Prinz
Howard Hughes Medical Institute · USInstitute of Molecular and Cell Biology · RUNankai University · CNNational Institute of Diabetes and Digestive and Kidney Diseases · US

Funding

Biogenesis of the endoplasmic reticulumZIADK060105 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI PRINZ, WILLIAM · 2009 to 2022
$8.5M
Biophysics of Macromolecular ComplexesZIADK033007 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2024
$4.9M
Howard Hughes Medical InstituteIntramural NIH HHS
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) forms a network of tubules and sheets that requires homotypic membrane fusion to be maintained. In metazoans, this process is mediated by dynamin-like guanosine triphosphatases (GTPases) called atlastins (ATLs), which are also required to maintain ER morphology. Previous work suggested that the dynamin-like GTPase Sey1p was needed to maintain ER morphology in Saccharomyces cerevisiae. In this paper, we demonstrate that Sey1p, like ATLs, mediates homotypic ER fusion. The absence of Sey1p resulted in the ER undergoing delayed fusion in vivo and proteoliposomes containing purified Sey1p fused in a GTP-dependent manner in vitro. Sey1p could be partially replaced by ATL1 in vivo. Like ATL1, Sey1p underwent GTP-dependent dimerization. We found that the residual ER-ER fusion that occurred in cells lacking Sey1p required the ER SNARE Ufe1p. Collectively, our results show that Sey1p and its homologues function analogously to ATLs in mediating ER fusion. They also indicate that S. cerevisiae has an alternative fusion mechanism that requires ER SNAREs.

Indexed as

Endoplasmic ReticulumGene Knockout TechniquesGTP-Binding ProteinsMembrane FusionMembrane ProteinsQa-SNARE ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsATL1 protein, humanGTP-Binding ProteinsMembrane ProteinsQa-SNARE ProteinsSaccharomyces cerevisiae ProteinsSEY1 protein, S cerevisiaeUFE1 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID22508509
PMCPMC3328390
OpenAlexW1990571611

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.