Evidence map›Paper›PMID 28358007›Full record

ArticleNature communications2017

Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structure.

Garima Jaipuria, Andrei Leonov, Karin Giller, Suresh Kumar Vasa, Łukasz Jaremko, Mariusz Jaremko, Rasmus Linser, Stefan Becker, Markus Zweckstetter

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.6field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  5. Increased [Biomolecules · 2025
    Article
  6. Cholesterol-dependent enzyme activity of human TSPO1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Review
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  10. Review
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  14. Review
  15. Review
  16. Article
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  18. Cellular sources of TSPO expression in healthy and diseased brain.European journal of nuclear medicine and molecular imaging · 2021
    Review
  19. Article
  20. Article
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

9 authors at 3 institutions in 1 country.

Garima JaipuriaDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075 Göttingen, Germany.
Andrei LeonovMax-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.
Karin GillerMax-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.
Suresh Kumar VasaMax-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.
Łukasz JaremkoDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075 Göttingen, Germany.
Mariusz JaremkoMax-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.
Rasmus LinserMax-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.
Stefan BeckerMax-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany.
Markus ZweckstetterDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Von-Siebold-Strasse 3a, 37075 Göttingen, Germany.
Max Planck Institute for Biophysical Chemistry · DEGerman Center for Neurodegenerative Diseases · DEUniversity of Göttingen · DE

Funding

European Research Council 282008
6 · The paper itself

Abstract

Cholesterol is an important regulator of membrane protein function. However, the exact mechanisms involved in this process are still not fully understood. Here we study how the tertiary and quaternary structure of the mitochondrial translocator protein TSPO, which binds cholesterol with nanomolar affinity, is affected by this sterol. Residue-specific analysis of TSPO by solid-state NMR spectroscopy reveals a dynamic monomer-dimer equilibrium of TSPO in the membrane. Binding of cholesterol to TSPO's cholesterol-recognition motif leads to structural changes across the protein that shifts the dynamic equilibrium towards the translocator monomer. Consistent with an allosteric mechanism, a mutation within the oligomerization interface perturbs transmembrane regions located up to 35 Å away from the interface, reaching TSPO's cholesterol-binding motif. The lower structural stability of the intervening transmembrane regions provides a mechanistic basis for signal transmission. Our study thus reveals an allosteric signal pathway that connects membrane protein tertiary and quaternary structure with cholesterol binding.

Indexed as

Allosteric RegulationAmino Acid SequenceAnimalsCell MembraneCholesterolLipid BilayersMagnetic Resonance SpectroscopyMiceMitochondriaProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiaryReceptors, GABASignal TransductionBzrp protein, mouseCholesterolLipid BilayersReceptors, GABA

Identifiers

PMID28358007
PMCPMC5379104
OpenAlexW2601080948

What OpenQuestion holds

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Registered trials

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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.