Evidence map›Paper›PMID 30871176›Full record

ReviewCells2019

Tubulin βII and βIII Isoforms as the Regulators of VDAC Channel Permeability in Health and Disease.

Marju Puurand, Kersti Tepp, Natalja Timohhina, Jekaterina Aid, Igor Shevchuk, Vladimir Chekulayev, Tuuli Kaambre

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. Pooled it
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  5. Chronically Established ρJournal of Cancer · 2026
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  14. 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
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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

7 authors at 1 institution in 1 country.

Marju PuurandLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. marju.puurand@kbfi.ee.ORCID 0000-0002-0083-3390
Kersti TeppLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. kersti.tepp@kbfi.ee.ORCID 0000-0001-7367-6632
Natalja TimohhinaLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. natalja.timohhina@kbfi.ee.
Jekaterina AidLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. jekaterina.aid@gmail.com.
Igor ShevchukLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. igor@chemnet.ee.
Vladimir ChekulayevLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. vladimir@chemnet.ee.
Tuuli KaambreLaboratory of Chemical Biology, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, 12618 Tallinn, Estonia. tuuli.kaambre@kbfi.ee.
National Institute of Chemical Physics and Biophysics · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent decades, there have been several models describing the relationships between the cytoskeleton and the bioenergetic function of the cell. The main player in these models is the voltage-dependent anion channel (VDAC), located in the mitochondrial outer membrane. Most metabolites including respiratory substrates, ADP, and Pi enter mitochondria only through VDAC. At the same time, high-energy phosphates are channeled out and directed to cellular energy transfer networks. Regulation of these energy fluxes is controlled by β-tubulin, bound to VDAC. It is also thought that β-tubulin‒VDAC interaction modulates cellular energy metabolism in cancer, e.g., switching from oxidative phosphorylation to glycolysis. In this review we focus on the described roles of unpolymerized αβ-tubulin heterodimers in regulating VDAC permeability for adenine nucleotides and cellular bioenergetics. We introduce the Mitochondrial Interactosome model and the function of the βII-tubulin subunit in this model in muscle cells and brain synaptosomes, and also consider the role of βIII-tubulin in cancer cells.

Indexed as

Cell Membrane PermeabilityDiseaseHealthHumansProtein IsoformsTubulinVoltage-Dependent Anion ChannelsProtein IsoformsTubulinVoltage-Dependent Anion Channelsbraincancercreatine kinasehexokinasemitochondriaoxidative muscleoxidative phosphorylationsynaptosomestubulinvoltage-dependent anion channel (VDAC)

Identifiers

PMID30871176
PMCPMC6468622
OpenAlexW2921446988

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.