Evidence map›Paper›PMID 29366674›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Cardiolipin dynamics and binding to conserved residues in the mitochondrial ADP/ATP carrier.

Anna L Duncan, Jonathan J Ruprecht, Edmund R S Kunji, Alan J Robinson

Open access · hybridAbstract read
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 66 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

4 authors at 2 institutions in 1 country.

Anna L DuncanMedical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.
Jonathan J RuprechtMedical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.
Edmund R S KunjiMedical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK.
Alan J RobinsonMedical Research Council, Mitochondrial Biology Unit, Cambridge Biomedical Campus, Cambridge CB2 0XY, UK. Electronic address: ajr@mrc-mbu.cam.ac.uk.
MRC Mitochondrial Biology Unit · GBMedical Research Council · GB

Funding

Medical Research Council MC_U105663139Medical Research Council MC_U105674181Medical Research Council MC_UU_00015/1
6 · The paper itself

Abstract

Cardiolipin in eukaryotes is found in the mitochondrial inner membrane, where it interacts with membrane proteins and, although not essential, is necessary for the optimal activity of a number of proteins. One of them is the mitochondrial ADP/ATP carrier, which imports ADP into the mitochondrion and exports ATP. In the crystal structures, cardiolipin is bound to three equivalent sites of the ADP/ATP carrier, but its role is unresolved. Conservation of residues at these cardiolipin binding sites across other members of the mitochondrial carrier superfamily indicates cardiolipin binding is likely to be important for the function of all mitochondrial carriers. Multiscale simulations were performed in a cardiolipin-containing membrane to investigate the dynamics of cardiolipin around the yeast and bovine ADP/ATP carriers in a lipid bilayer and the properties of the cardiolipin-binding sites. In coarse-grain simulations, cardiolipin molecules bound to the carriers for longer periods of time than phosphatidylcholine and phosphatidylethanolamine lipids-with timescales in the tens of microseconds. Three long-lived cardiolipin binding sites overlapped with those in the crystal structures of the carriers. Other shorter-lived cardiolipin interaction sites were identified in both membrane leaflets. However, the timescales of the interactions were of the same order as phosphatidylcholine and phosphatidylethanolamine, suggesting that these sites are not specific for cardiolipin binding. The calculation of lipid binding times and the overlap of the cardiolipin binding sites between the structures and simulations demonstrate the potential of multiscale simulations to investigate the dynamics and behavior of lipids interacting with membrane proteins.

Indexed as

Protein Interaction Domains and MotifsAmino Acid SequenceAnimalsBinding SitesCardiolipinsCattleConserved SequenceMitochondriaMitochondrial ADP, ATP TranslocasesMitochondrial MembranesModels, MolecularMolecular Dynamics SimulationProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCardiolipinsMitochondrial ADP, ATP TranslocasesSaccharomyces cerevisiae ProteinsAdenine nucleotide translocatorAdenine nucleotide transporterCardiolipinMitochondriaMolecular dynamics simulationTrimethyllysine

Identifiers

PMID29366674
PMCPMC5988563
OpenAlexW2789358625

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.