Evidence map›Paper›PMID 31816638›Full record

ArticleThe Journal of general physiology2020

Highly coupled transport can be achieved in free-exchange transport models.

Grant A Hussey, Nathan E Thomas, Katherine A Henzler-Wildman

Abstract read
In one paragraph

Article in The Journal of general physiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. Multimodal dynamics control activity of a glial glutamate transporter.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. A Small Multidrug Resistance Transporter inbioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Microsecond Motion of the Bacterial Transporter EmrE in Lipid Bilayers.Journal of the American Chemical Society · 2023
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Kinetic model for reversible radical transfer in ribonucleotide reductase.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Review
  19. Multiscale kinetic analysis of proteins.Current opinion in structural biology · 2022
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Grant A Hussey
Nathan E ThomasDepartment of Biochemistry, University of Wisconsin at Madison, Madison, WI.
Katherine A Henzler-WildmanDepartment of Biochemistry, University of Wisconsin at Madison, Madison, WI.

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
TRANSPORT MECHANISM OF THE MULTIDRUG RESISTANCE EFFLUX PROTEIN, EMRER01GM095839 · NIGMS · WASHINGTON UNIVERSITY · PI HENZLER-WILDMAN, KATHERINE ANNE · 2011 to 2020
$3.1M
NIGMS NIH HHS R01 GM095839NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Secondary active transporters couple the transport of an ion species down its concentration gradient to the uphill transport of another substrate. Despite the importance of secondary active transport to multidrug resistance, metabolite transport, and nutrient acquisition, among other biological processes, the microscopic steps of the coupling mechanism are not well understood. Often, transport models illustrate coupling mechanisms through a limited number of "major" conformations or states, yet recent studies have indicated that at least some transporters violate these models. The small multidrug resistance transporter EmrE has been shown to couple proton influx to multidrug efflux via a mechanism that incorporates both "major" and "minor" conformational states and transitions. The resulting free exchange transport model includes multiple leak pathways and theoretically allows for both exchange and cotransport of ion and substrate. To better understand how coupled transport can be achieved in such a model, we numerically simulate a free-exchange model of transport to determine the step-by-step requirements for coupled transport. We find that only moderate biasing of rate constants for key transitions produce highly efficient net transport approaching a perfectly coupled, stoichiometric model. We show how a free-exchange model can enable complex phenotypes, including switching transport direction with changing environmental conditions or substrates. This research has broad implications for synthetic biology, as it demonstrates the utility of free-exchange transport models and the fine tuning required for perfectly coupled transport.

Indexed as

Models, TheoreticalAntiportersEscherichia coli ProteinsIon TransportKineticsProtonsAntiportersEmrE protein, E coliEscherichia coli ProteinsProtons

Identifiers

PMID31816638
PMCPMC7034097

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.