Evidence map›Paper›PMID 28356327›Full record

ArticleThe Journal of cell biology2017

The crossover conformational shift of the GTPase atlastin provides the energy driving ER fusion.

James Winsor, David D Hackney, Tina H Lee

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  3. Article
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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

3 authors at 1 institution in 1 country.

James WinsorDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213.ORCID 0000-0002-9673-4839
David D HackneyDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213.ORCID 0000-0003-2929-8165
Tina H LeeDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213 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

The homotypic fusion of endoplasmic reticulum membranes is catalyzed by the atlastin GTPase. The mechanism involves trans-dimerization between GTPase heads and a favorable crossover conformational shift, catalyzed by GTP hydrolysis, that converts the dimer from a "prefusion" to "postfusion" state. However, whether crossover formation actually energizes fusion remains unclear, as do the sequence of events surrounding it. Here, we made mutations in atlastin to selectively destabilize the crossover conformation and used fluorescence-based kinetic assays to analyze the variants. All variants underwent dimerization and crossover concurrently, and at wild-type rates. However, certain variants were unstable once in the crossover dimer conformation, and crossover dimer stability closely paralleled lipid-mixing activity. Tethering, however, appeared to be unimpaired in all mutant variants. The results suggest that tethering and lipid mixing are catalyzed concurrently by GTP hydrolysis but that the energy requirement for lipid mixing exceeds that for tethering, and the full energy released through crossover formation is necessary for fusion.

Indexed as

AnimalsBiocatalysisChlorocebus aethiopsCOS CellsEndoplasmic ReticulumFluorescenceGTP-Binding ProteinsKineticsMembrane ProteinsModels, MolecularMutationProtein ConformationATL1 protein, humanGTP-Binding ProteinsMembrane Proteins

Identifiers

PMID28356327
PMCPMC5412568
OpenAlexW2601957356

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.