Evidence map›Paper›PMID 18654841›Full record

ReviewJournal of bioenergetics and biomembranes2008

VDAC regulation: role of cytosolic proteins and mitochondrial lipids.

Tatiana K Rostovtseva, Sergey M Bezrukov

Open access · greenAbstract readReview
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

108 citing papers in PubMed, 209 citations in OpenAlex.

  1. Trial
  2. Increased Expression of Desmin and Vimentin Impairs Mitochondrial Function and Reduces Contractility via G0S2 in Bladder Smooth Muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Review
  4. Elliptical β-barrel deformation underlies gating in VDAC1.Protein science : a publication of the Protein Society · 2026
    Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. How cytoskeletal proteins regulate mitochondrial energetics in cell physiology and diseases.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. A C-Terminally Truncated Variant ofFrontiers in physiology · 2021
    Article
  18. Review
  19. Review
  20. MicroED structure of lipid-embedded mammalian mitochondrial voltage-dependent anion channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article

48 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

2 authors at 1 institution in 1 country.

Tatiana K RostovtsevaLaboratory of Physical and Structural Biology, Program in Physical Biology, NICHD, National Institutes of Health, Rockville Pike, Bethesda, MD 20892, USA. rostovtt@mail.nih.gov
Sergey M Bezrukov
National Institutes of Health · US

Funding

Biophysics of Large Membrane ChannelsZIAHD000072 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BEZRUKOV, SERGEY M · 2009 to 2025
$22.8M
Intramural NIH HHS Z99 HD999999
6 · The paper itself

Abstract

It was recently asserted that the voltage-dependent anion channel (VDAC) serves as a global regulator, or governor, of mitochondrial function (Lemasters and Holmuhamedov, Biochim Biophys Acta 1762:181-190, 2006). Indeed, VDAC, positioned on the interface between mitochondria and the cytosol (Colombini, Mol Cell Biochem 256:107-115, 2004), is at the control point of mitochondria life and death. This large channel plays the role of a "switch" that defines in which direction mitochondria will go: to normal respiration or to suppression of mitochondria metabolism that leads to apoptosis and cell death. As the most abundant protein in the mitochondrial outer membrane (MOM), VDAC is known to be responsible for ATP/ADP exchange and for the fluxes of other metabolites across MOM. It controls them by switching between the open and "closed" states that are virtually impermeable to ATP and ADP. This control has dual importance: in maintaining normal mitochondria respiration and in triggering apoptosis when cytochrome c and other apoptogenic factors are released from the intermembrane space into the cytosol. Emerging evidence indicates that VDAC closure promotes apoptotic signals without direct involvement of VDAC in the permeability transition pore or hypothetical Bax-containing cytochrome c permeable pores. VDAC gating has been studied extensively for the last 30 years on reconstituted VDAC channels. In this review we focus exclusively on physiologically relevant regulators of VDAC gating such as endogenous cytosolic proteins and mitochondrial lipids. Closure of VDAC induced by such dissimilar cytosolic proteins as pro-apoptotic tBid and dimeric tubulin is compared to show that the involved mechanisms are rather distinct. While tBid mostly modulates VDAC voltage gating, tubulin blocks the channel with the efficiency of blockage controlled by voltage. We also discuss how characteristic mitochondrial lipids, phospatidylethanolamine and cardiolipin, could regulate VDAC gating. Overall, we demonstrate that VDAC gating is not just an observation made under artificial conditions of channel reconstitution but is a major mechanism of MOM permeability control.

Indexed as

ApoptosisBH3 Interacting Domain Death Agonist ProteinCardiolipinsCytochromes cCytosolIon Channel GatingMitochondrial MembranesMitochondrial ProteinsPhosphatidylethanolaminesVoltage-Dependent Anion ChannelsBH3 Interacting Domain Death Agonist ProteinCardiolipinsCytochromes cMitochondrial ProteinsphosphatidylethanolaminePhosphatidylethanolaminesVoltage-Dependent Anion Channels

Identifiers

PMID18654841
PMCPMC2671000
OpenAlexW2030349442

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.