Evidence map›Paper›PMID 36102950›Full record

ReviewThe Journal of membrane biology2022

Lipid and Lipidation in Membrane Fusion.

Avijit Sardar, Nikesh Dewangan, Bishvanwesha Panda, Debosmita Bhowmick, Pradip K Tarafdar

Abstract readReview
In one paragraph

Review in The Journal of membrane biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Extracellular Vesicles fromNanomaterials (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Review
  7. Decoding the Role of Lipid Metabolism and Membrane Dynamics in Melanoma.International journal of molecular sciences · 2026
    Review
  8. Review
  9. Article
  10. Review
  11. Membrane-Targeting Antivirals.International journal of molecular sciences · 2025
    Review
  12. Review
  13. Trehalose dimycolate inhibits phagosome maturation and promotes intracellularProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    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.

Avijit SardarIndian Institute of Science Education and Research Kolkata, Nadia, Mohanpur, West Bengal, 741246, India.
Nikesh DewanganIndian Institute of Science Education and Research Kolkata, Nadia, Mohanpur, West Bengal, 741246, India.
Bishvanwesha PandaIndian Institute of Science Education and Research Kolkata, Nadia, Mohanpur, West Bengal, 741246, India.
Debosmita BhowmickIndian Institute of Science Education and Research Kolkata, Nadia, Mohanpur, West Bengal, 741246, India.
Pradip K TarafdarIndian Institute of Science Education and Research Kolkata, Nadia, Mohanpur, West Bengal, 741246, India. tarafdar@iiserkol.ac.in.ORCID 0000-0002-1059-950X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane fusion plays a lead role in the transport of vesicles, neurotransmission, mitochondrial dynamics, and viral infection. There are fusion proteins that catalyze and regulate the fusion. Interestingly, various types of fusion proteins are present in nature and they possess diverse mechanisms of action. We have highlighted the importance of the functional domains of intracellular heterotypic fusion, homotypic endoplasmic reticulum (ER), homotypic mitochondrial, and type-I viral fusion. During intracellular heterotypic fusion, the SNAREs and four-helix bundle formation are prevalent. Type-I viral fusion is controlled by the membrane destabilizing properties of fusion peptide and six-helix bundle formation. The ER/mitochondrial homotypic fusion is controlled by GTPase activity and the membrane destabilization properties of the amphipathic helix(s). Although the mechanism of action of these fusion proteins is diverse, they have some similarities. In all cases, the lipid composition of the membrane greatly affects membrane fusion. Next, examples of lipidation of the fusion proteins were discussed. We suggest that the fatty acyl hydrophobic tail not only acts as an anchor but may also modulate the energetics of membrane fusion intermediates. Lipidation is also important to design more effective peptide-based fusion inhibitors. Together, we have shown that membrane lipid composition and lipidation are important to modulate membrane fusion.

Indexed as

GTP PhosphohydrolasesMembrane FusionEndoplasmic ReticulumLipidsMitochondrial DynamicsGTP PhosphohydrolasesLipidsAtlastinsFusion inhibitorMitofusinsPalmitoylationSNAREsViral fusion

Identifiers

PMID36102950
PMCPMC9472184

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.