Evidence map›Paper›PMID 25555915›Full record

ArticleThe Journal of biological chemistry2015

The Atlastin C-terminal tail is an amphipathic helix that perturbs the bilayer structure during endoplasmic reticulum homotypic fusion.

Joseph E Faust, Tanvi Desai, Avani Verma, Idil Ulengin, Tzu-Lin Sun, Tyler J Moss, Miguel A Betancourt-Solis, Huey W Huang, Tina Lee, James A McNew

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 54 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. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The atlastin paralogs: The complexity in the tails.The Journal of cell biology · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Frontiers in neuroscience · 2020
    Article
  20. 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 2 institutions in 1 country.

Joseph E FaustDepartment of Biochemistry and Cell Biology, Rice University, Houston Texas 77005.
Tanvi DesaiDepartment of Biochemistry and Cell Biology, Rice University, Houston Texas 77005.
Avani VermaDepartment of Biochemistry and Cell Biology, Rice University, Houston Texas 77005.
Idil UlenginDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Tzu-Lin SunDepartment of Physics and Astronomy, Rice University, Houston, Texas 77005.
Tyler J MossDepartment of Biochemistry and Cell Biology, Rice University, Houston Texas 77005.
Miguel A Betancourt-SolisDepartment of Biochemistry and Cell Biology, Rice University, Houston Texas 77005.
Huey W HuangDepartment of Physics and Astronomy, Rice University, Houston, Texas 77005.
Tina LeeDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
James A McNewDepartment of Biochemistry and Cell Biology, Rice University, Houston Texas 77005,. Electronic address: mcnew@rice.edu.
Rice University · USCarnegie Mellon University · US

Funding

Membrane-active Peptides and ProteinsR01GM055203 · NIGMS · RICE UNIVERSITY · PI HUANG, HUEY W. · 1997 to 2017
$5.0M
Mechanism and Role of Membrane Fusion by the Atlastin GTPase - Equipment SupplementR01GM107285 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LEE, CHRISTINA H · 2014 to 2025
$2.9M
Biochemical analysis of the ER fusion protein allastinR01GM101377 · NIGMS · RICE UNIVERSITY · PI MCNEW, JAMES A · 2012 to 2015
$1.1M
NIGMS NIH HHS GM101377NIGMS NIH HHS GM107285NIGMS NIH HHS GM55203NIGMS NIH HHS R01 GM101377NIGMS NIH HHS R01 GM107285
6 · The paper itself

Abstract

Fusion of tubular membranes is required to form three-way junctions found in reticular subdomains of the endoplasmic reticulum. The large GTPase Atlastin has recently been shown to drive endoplasmic reticulum membrane fusion and three-way junction formation. The mechanism of Atlastin-mediated membrane fusion is distinct from SNARE-mediated membrane fusion, and many details remain unclear. In particular, the role of the amphipathic C-terminal tail of Atlastin is still unknown. We found that a peptide corresponding to the Atlastin C-terminal tail binds to membranes as a parallel α helix, induces bilayer thinning, and increases acyl chain disorder. The function of the C-terminal tail is conserved in human Atlastin. Mutations in the C-terminal tail decrease fusion activity in vitro, but not GTPase activity, and impair Atlastin function in vivo. In the context of unstable lipid bilayers, the requirement for the C-terminal tail is abrogated. These data suggest that the C-terminal tail of Atlastin locally destabilizes bilayers to facilitate membrane fusion.

Indexed as

Membrane FusionAnimalsDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumGTP-Binding ProteinsGTP PhosphohydrolasesHumansLipid BilayersMembrane ProteinsProtein Structure, SecondaryATL1 protein, humanatl protein, DrosophilaDrosophila ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesLipid BilayersMembrane ProteinsCell CompartmentalizationEndoplasmic Reticulum (ER)FRETGTPaseMembrane FusionMembrane StructureNeurodegenerationPhospholipid Vesicle

Identifiers

PMID25555915
PMCPMC4335215
OpenAlexW1997558271

What OpenQuestion holds

Textmetadata
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.