Evidence map›Paper›PMID 25253720›Full record

ArticleMolecular biology of the cell2014

Membrane tethering by the atlastin GTPase depends on GTP hydrolysis but not on forming the cross-over configuration.

Simran G Saini, Chuang Liu, Peijun Zhang, Tina H Lee

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Membrane fusion byMolecular biology of the cell · 2022
    Article
  4. 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
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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

4 authors at 2 institutions in 1 country.

Simran G SainiDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213.
Chuang LiuDepartment of Structural Biology, University of Pittsburgh, Pittsburgh, PA 15260.
Peijun ZhangDepartment of Structural Biology, University of Pittsburgh, Pittsburgh, PA 15260.
Tina H LeeDepartment of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213 thl@andrew.cmu.edu.
Carnegie Mellon University · USUniversity of Pittsburgh · 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
Structure and function of membrane receptor signaling complex in bacterial chemotR01GM085043 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHANG, PEIJUN · 2009 to 2013
$1.4M
NIDDK NIH HHS 1R21DK088208NIGMS NIH HHS GM085043NIGMS NIH HHS R01 GM085043NIGMS NIH HHS R01 GM107285NIGMS NIH HHS R01GM107285
6 · The paper itself

Abstract

The membrane-anchored atlastin GTPase couples nucleotide hydrolysis to the catalysis of homotypic membrane fusion to form a branched endoplasmic reticulum network. Trans dimerization between atlastins anchored in opposing membranes, accompanied by a cross-over conformational change, is thought to draw the membranes together for fusion. Previous studies on the conformational coupling of atlastin to its GTP hydrolysis cycle have been carried out largely on atlastins lacking a membrane anchor. Consequently, whether fusion involves a discrete tethering step and, if so, the potential role of GTP hydrolysis and cross-over in tethering remain unknown. In this study, we used membrane-anchored atlastins in assays that separate tethering from fusion to dissect the requirements for each. We found that tethering depended on GTP hydrolysis, but, unlike fusion, it did not depend on cross-over. Thus GTP hydrolysis initiates stable head-domain contact in trans to tether opposing membranes, whereas cross-over formation plays a more pivotal role in powering the lipid rearrangements for fusion.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsCOS CellsCryoelectron MicroscopyDrosophila ProteinsEndoplasmic ReticulumGTP PhosphohydrolasesGuanosine TriphosphateHydrolysisMembrane FusionMicroscopy, FluorescenceModels, BiologicalModels, MolecularMutationProtein Bindingatl protein, DrosophilaDrosophila ProteinsGTP PhosphohydrolasesGuanosine Triphosphate

Identifiers

PMID25253720
PMCPMC4244202
OpenAlexW2008218993

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.