Evidence map›Paper›PMID 25305015›Full record

ArticleThe Journal of biological chemistry2014

An annular lipid belt is essential for allosteric coupling and viral inhibition of the antigen translocation complex TAP (transporter associated with antigen processing).

Sabine Eggensperger, Olivier Fisette, David Parcej, Lars V Schäfer, Robert Tampé

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 29 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

5 authors at 2 institutions in 1 country.

Sabine EggenspergerFrom the Institute of Biochemistry, Biocenter, Goethe University, Max-von-Laue-Strasse 9, 60438 Frankfurt/M..
Olivier Fisettethe Lehrstuhl für Theoretische Chemie, Ruhr-University Bochum, 44780 Bochum, and.
David ParcejFrom the Institute of Biochemistry, Biocenter, Goethe University, Max-von-Laue-Strasse 9, 60438 Frankfurt/M..
Lars V Schäferthe Lehrstuhl für Theoretische Chemie, Ruhr-University Bochum, 44780 Bochum, and.
Robert TampéFrom the Institute of Biochemistry, Biocenter, Goethe University, Max-von-Laue-Strasse 9, 60438 Frankfurt/M., the Cluster of Excellence-Macromolecular Complexes, Goethe University, Max-von-Laue-Str. 9, 60438 Frankfurt/M., Germany tampe@em.uni-frankfurt.de.
Ruhr University Bochum · DEGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transporter associated with antigen processing (TAP) constitutes a focal element in the adaptive immune response against infected or malignantly transformed cells. TAP shuttles proteasomal degradation products into the lumen of the endoplasmic reticulum for loading of major histocompatibility complex (MHC) class I molecules. Here, the heterodimeric TAP complex was purified and reconstituted in nanodiscs in defined stoichiometry. We demonstrate that a single heterodimeric core-TAP complex is active in peptide binding, which is tightly coupled to ATP hydrolysis. Notably, with increasing peptide length, the ATP turnover was gradually decreased, revealing that ATP hydrolysis is coupled to the movement of peptide through the ATP-binding cassette transporter. In addition, all-atom molecular dynamics simulations show that the observed 22 lipids are sufficient to form an annular belt surrounding the TAP complex. This lipid belt is essential for high affinity inhibition by the herpesvirus immune evasin ICP47. In conclusion, nanodiscs are a powerful approach to study the important role of lipids as well as the function, interaction, and modulation of the antigen translocation machinery.

Indexed as

Antigen PresentationAdenosine TriphosphatasesAdenosine TriphosphateCell Line, TumorHistocompatibility Antigens Class IHumansImmediate-Early ProteinsMembrane LipidsMultiprotein ComplexesPeptidesProteasome Endopeptidase ComplexProtein TransportAdenosine TriphosphatasesAdenosine TriphosphateHistocompatibility Antigens Class IICP47 protein, Herpes simplex virusImmediate-Early ProteinsMembrane LipidsMultiprotein ComplexesPeptidesProteasome Endopeptidase ComplexAntigen ProcessingATP-binding Cassette TransporterHerpesvirusLipid BilayerMembrane ProteinMembrane TransportMembrane Transporter ReconstitutionPeptide TransportTransporter

Identifiers

PMID25305015
PMCPMC4246070
OpenAlexW2166585484

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.