Evidence map›Paper›PMID 30249723›Full record

ArticleThe Journal of cell biology2018

GTP hydrolysis promotes disassembly of the atlastin crossover dimer during ER fusion.

James Winsor, Ursula Machi, Qixiu Han, David D Hackney, Tina H Lee

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 33% 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

13 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Rab10 Promotes Atlastin-Mediated Endoplasmic Reticulum Membrane Fusion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Membrane fusion byMolecular biology of the cell · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
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

5 authors at 1 institution in 1 country.

James WinsorDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA.ORCID 0000-0002-9673-4839
Ursula MachiDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA.ORCID 0000-0002-5360-1980
Qixiu HanDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA.ORCID 0000-0001-9268-3467
David D HackneyDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA.ORCID 0000-0003-2929-8165
Tina H LeeDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA thl@andrew.cmu.edu.ORCID 0000-0002-2610-6204
Carnegie Mellon University · US

Funding

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
NIGMS NIH HHS R01 GM107285
6 · The paper itself

Abstract

Membrane fusion of the ER is catalyzed when atlastin GTPases anchored in opposing membranes dimerize and undergo a crossed over conformational rearrangement that draws the bilayers together. Previous studies have suggested that GTP hydrolysis triggers crossover dimerization, thus directly driving fusion. In this study, we make the surprising observations that WT atlastin undergoes crossover dimerization before hydrolyzing GTP and that nucleotide hydrolysis and Pi release coincide more closely with dimer disassembly. These findings suggest that GTP binding, rather than its hydrolysis, triggers crossover dimerization for fusion. In support, a new hydrolysis-deficient atlastin variant undergoes rapid GTP-dependent crossover dimerization and catalyzes fusion at an initial rate similar to WT atlastin. However, the variant cannot sustain fusion activity over time, implying a defect in subunit recycling. We suggest that GTP binding induces an atlastin conformational change that favors crossover dimerization for fusion and that the input of energy from nucleotide hydrolysis promotes complex disassembly for subunit recycling.

Indexed as

Membrane FusionProtein MultimerizationEndoplasmic ReticulumGTP-Binding ProteinsGuanosine TriphosphateHumansHydrolysisMembrane ProteinsATL1 protein, humanGTP-Binding ProteinsGuanosine TriphosphateMembrane Proteins

Identifiers

PMID30249723
PMCPMC6279388
OpenAlexW2891888829

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.