Evidence map›Paper›PMID 22802620›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Lipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion.

Tina Y Liu, Xin Bian, Sha Sun, Xiaoyu Hu, Robin W Klemm, William A Prinz, Tom A Rapoport, Junjie Hu

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
5.2field-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

80 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. 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
  6. Article
  7. Article
  8. Article
  9. Review
  10. The atlastin paralogs: The complexity in the tails.The Journal of cell biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Lipid and Lipidation in Membrane Fusion.The Journal of membrane biology · 2022
    Review
  18. Article
  19. Article
  20. Article

20 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

8 authors at 3 institutions in 2 countries.

Tina Y LiuHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA 02115.
Xin Bian
Sha Sun
Xiaoyu Hu
Robin W Klemm
William A Prinz
Tom A Rapoport
Junjie Hu
Nankai University · CNHarvard University · USNational Institutes of Health · 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
Howard Hughes Medical Institute
6 · The paper itself

Abstract

The homotypic fusion of endoplasmic reticulum (ER) membranes is mediated by atlastin (ATL), which consists of an N-terminal cytosolic domain containing a GTPase module and a three-helix bundle followed by two transmembrane (TM) segments and a C-terminal tail (CT). Fusion depends on a GTP hydrolysis-induced conformational change in the cytosolic domain. Here, we show that the CT and TM segments also are required for efficient fusion and provide insight into their mechanistic roles. The essential feature of the CT is a conserved amphipathic helix. A synthetic peptide corresponding to the helix, but not to unrelated amphipathic helices, can act in trans to restore the fusion activity of tailless ATL. The CT promotes vesicle fusion by interacting directly with and perturbing the lipid bilayer without causing significant lysis. The TM segments do not serve as mere membrane anchors for the cytosolic domain but rather mediate the formation of ATL oligomers. Point mutations in either the C-terminal helix or the TMs impair ATL's ability to generate and maintain ER morphology in vivo. Our results suggest that protein-lipid and protein-protein interactions within the membrane cooperate with the conformational change of the cytosolic domain to achieve homotypic ER membrane fusion.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsCircular DichroismDrosophila melanogasterDrosophila ProteinsElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumEscherichia coliFluoresceinsFluorescence Resonance Energy TransferGene ComponentsGTP PhosphohydrolasesHumansImmunoprecipitationLipid Metabolismatl protein, DrosophilaDrosophila ProteinsFluoresceinsfluorexonGTP PhosphohydrolasesLiposomes

Identifiers

PMID22802620
PMCPMC3420179
OpenAlexW2009098062

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.