Evidence map›Paper›PMID 25646430›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Single liposome analysis of peptide translocation by the ABC transporter TAPL.

Tina Zollmann, Gemma Moiset, Franz Tumulka, Robert Tampé, Bert Poolman, Rupert Abele

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Interdomain communication in a homodimeric ABC transporter.The Journal of biological chemistry · 2024
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Moving the Cellular Peptidome by Transporters.Frontiers in cell and developmental biology · 2018
    Review
  16. Crystal structure and mechanistic basis of a functional homolog of the antigen transporter TAP.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Review
  18. Article
  19. Article
  20. Review
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

6 authors at 2 institutions in 2 countries.

Tina ZollmannInstitute of Biochemistry and.
Gemma MoisetDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands.
Franz TumulkaInstitute of Biochemistry and.
Robert TampéInstitute of Biochemistry and Cluster of Excellence Frankfurt Macromolecular Complexes, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany; and.
Bert PoolmanDepartment of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands abele@em.uni-frankfurt.de B.Poolman@rug.nl.
Rupert AbeleInstitute of Biochemistry and abele@em.uni-frankfurt.de B.Poolman@rug.nl.
University of Groningen · NLGoethe University Frankfurt · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP-binding cassette (ABC) transporters use ATP to drive solute transport across biological membranes. Members of this superfamily have crucial roles in cell physiology, and some of the transporters are linked to severe diseases. However, understanding of the transport mechanism, especially of human ABC exporters, is scarce. We reconstituted the human lysosomal polypeptide ABC transporter TAPL, expressed in Pichia pastoris, into lipid vesicles (liposomes) and performed explicit transport measurements. We analyzed solute transport at the single liposome level by monitoring the coincident fluorescence of solutes and proteoliposomes in the focal volume of a confocal microscope. We determined a turnover number of eight peptides per minute, which is two orders of magnitude higher than previously estimated from macroscopic measurements. Moreover, we show that TAPL translocates peptides against a large concentration gradient. Maximal filling is not limited by an electrochemical gradient but by trans-inhibition. Countertransport and reversibility studies demonstrate that peptide translocation is a strictly unidirectional process. Altogether, these data are included in a refined model of solute transport by ABC exporters.

Indexed as

LiposomesATP-Binding Cassette TransportersHumansPeptidesPichiaProtein TransportRecombinant ProteinsATP-Binding Cassette TransportersLiposomesPeptidesRecombinant ProteinsABCB9DCFBAlysosometrans-inhibitionuphill transport

Identifiers

PMID25646430
PMCPMC4343155
OpenAlexW2166422114

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.