Evidence map›Paper›PMID 25209018›Full record

ReviewJournal of bioenergetics and biomembranes2014

The role of tubulin in the mitochondrial metabolism and arrangement in muscle cells.

Kersti Tepp, Kati Mado, Minna Varikmaa, Aleksandr Klepinin, Natalja Timohhina, Igor Shevchuk, Vladimir Chekulayev, Andrey V Kuznetsov, Rita Guzun, Tuuli Kaambre

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of bioenergetics and biomembranes, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 19 citations in OpenAlex.

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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

10 authors at 4 institutions in 3 countries.

Kersti TeppLaboratory of Bioenergetics, National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, Tallinn, 12618, Estonia, kersti.tepp@kbfi.ee.
Kati Mado
Minna Varikmaa
Aleksandr Klepinin
Natalja Timohhina
Igor Shevchuk
Vladimir Chekulayev
Andrey V Kuznetsov
Rita Guzun
Tuuli Kaambre
National Institute of Chemical Physics and Biophysics · EEInnsbruck Medical University · ATTallinn University of Technology · EEUniversité Joseph Fourier · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tubulin, a well-known component of the microtubule in the cytoskeleton, has an important role in the transport and positioning of mitochondria in a cell type dependent manner. This review describes different functional interactions of tubulin with cellular protein complexes and its functional interaction with the mitochondrial outer membrane. Tubulin is present in oxidative as well as glycolytic type muscle cells, but the kinetics of the in vivo regulation of mitochondrial respiration in these muscle types is drastically different. The interaction between VDAC and tubulin is probably influenced by such factors as isoformic patterns of VDAC and tubulin, post-translational modifications of tubulin and phosphorylation of VDAC. Important factor of the selective permeability of VDAC is the mitochondrial creatine kinase pathway which is present in oxidative cells, but is inactive or missing in glycolytic muscle and cancer cells. As the tubulin-VDAC interaction reduces the permeability of the channel by adenine nucleotides, energy transfer can then take place effectively only through the mitochondrial creatine kinase/phosphocreatine pathway. Therefore, closure of VDAC by tubulin may be one of the reasons of apoptosis in cells without the creatine kinase pathway. An important question in tubulin regulated interactions is whether other proteins are interacting with tubulin. The functional interaction may be direct, through other proteins like plectins, or influenced by simultaneous interaction of other complexes with VDAC.

Indexed as

AnimalsCytoskeletonHumansMitochondrial MembranesMitochondria, MuscleProtein BindingTubulinVoltage-Dependent Anion ChannelsTubulinVoltage-Dependent Anion Channels

Identifiers

PMID25209018
OpenAlexW2083388384

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.