Evidence map›Paper›PMID 26709731›Full record

ReviewThe FEBS journal2016

VDAC-2: Mitochondrial outer membrane regulator masquerading as a channel?

Svetlana Rajkumar Maurya, Radhakrishnan Mahalakshmi

Open access · greenAbstract readReview
In one paragraph

Review in The FEBS journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. VDAC2: an emerging pivotal and multifaceted regulator in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
  3. Article
  4. Time- and season-dependent changes in the steroidogenic markers in female tree sparrow (Passer montanus).Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Role of cysteines in mammalian VDAC isoforms' function.Biochimica et biophysica acta · 2016
    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

2 authors at 1 institution in 1 country.

Svetlana Rajkumar MauryaMolecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.
Radhakrishnan MahalakshmiMolecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.ORCID 0000-0003-1549-7550
Indian Institute of Science Education and Research, Bhopal · IN

Funding

DBT-Wellcome Trust India Alliance IA/I/14/1/501305Wellcome TrustWellcome Trust IA/I/14/1/501305
6 · The paper itself

Abstract

The voltage-dependent anion channels (VDACs) are the workforce of mitochondrial transport and as such are required for cellular metabolism. The elaborate interplay between mitochondria and the apoptotic pathway supports a role for VDACs as a major regulator of cell death. Although VDAC-1 has an established role in apoptosis and cell homeostasis, the role of VDAC-2 has been controversial. In humans, VDAC-2 is best known for its anti-apoptotic properties. In this Viewpoint, we associate the various functional studies on VDAC-2 with structural reports, to decode its unique behavior. The well-structured N-terminus, compact barrel form, differences in the loop regions, specific transmembrane segments and the abundance of thiols in VDAC-2 enable this isoform to perform a different subset of regulatory functions, establish anti-apoptotic features and contribute to gametogenesis. VDAC-2 structural features that demarcate it from VDAC-1 suggest that this particular isoform is better suited for regulating reactive oxygen species, steroidogenesis and mitochondria-associated endoplasmic reticulum membrane regulatory pathways, with ion transport forming a secondary role. A better understanding of the unique structural features of the VDAC family will aid in the design of inhibitors that could alleviate irregularities in VDAC-controlled pathways.

Indexed as

AnimalsHumansIon ChannelsMitochondrial MembranesVoltage-Dependent Anion Channel 2Ion ChannelsVDAC2 protein, humanVoltage-Dependent Anion Channel 2apoptosiscysteinesmitochondrial outer membranevoltage-dependent anion channelβ-barrel proteins

Identifiers

PMID26709731
PMCPMC6258906
OpenAlexW2216538777

What OpenQuestion holds

Textmetadata
LicenceTDM
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.