Evidence map›Paper›PMID 29615663›Full record

ArticleScientific reports2018

Low affinity uniporter carrier proteins can increase net substrate uptake rate by reducing efflux.

Evert Bosdriesz, Meike T Wortel, Jurgen R Haanstra, Marijke J Wagner, Pilar de la Torre Cortés, Bas Teusink

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

19 citing papers in PubMed, 41 citations in OpenAlex.

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  7. Perfect adaptation achieved by transport limitations governs the inorganic phosphate response inProceedings of the National Academy of Sciences of the United States of America · 2023
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  14. Development and quantitative analysis of a biosensor based on the Arabidopsis SWEET1 sugar transporter.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

6 authors at 4 institutions in 2 countries.

Evert BosdrieszSystems Bioinformatics, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University, Amsterdam, De Boelelaan 1108, 1081HZ, The Netherlands.ORCID 0000-0002-8788-9548
Meike T WortelSystems Bioinformatics, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University, Amsterdam, De Boelelaan 1108, 1081HZ, The Netherlands.ORCID 0000-0002-3191-2710
Jurgen R HaanstraSystems Bioinformatics, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University, Amsterdam, De Boelelaan 1108, 1081HZ, The Netherlands.ORCID 0000-0001-9652-0219
Marijke J WagnerSystems Bioinformatics, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University, Amsterdam, De Boelelaan 1108, 1081HZ, The Netherlands.
Pilar de la Torre CortésDepartment of Biotechnology, Delft University of Technology, Delft, The Netherlands.
Bas TeusinkSystems Bioinformatics, Amsterdam Institute for Molecules, Medicines and Systems (AIMMS), VU University, Amsterdam, De Boelelaan 1108, 1081HZ, The Netherlands. b.teusink@vu.nl.ORCID 0000-0003-3929-0423
Vrije Universiteit Amsterdam · NLDelft University of Technology · NLThe Netherlands Cancer Institute · NLUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many organisms have several similar transporters with different affinities for the same substrate. Typically, high-affinity transporters are expressed when substrate is scarce and low-affinity ones when it is abundant. The benefit of using low instead of high-affinity transporters remains unclear, especially when additional nutrient sensors are present. Here, we investigate two hypotheses. It was previously hypothesized that there is a trade-off between the affinity and the catalytic efficiency of transporters, and we find some but no definitive support for it. Additionally, we propose that for uptake by facilitated diffusion, at saturating substrate concentrations, lowering the affinity enhances the net uptake rate by reducing substrate efflux. As a consequence, there exists an optimal, external-substrate-concentration dependent transporter affinity. A computational model of Saccharomyces cerevisiae glycolysis shows that using the low affinity HXT3 transporter instead of the high affinity HXT6 enhances the steady-state flux by 36%. We tried to test this hypothesis with yeast strains expressing a single glucose transporter modified to have either a high or a low affinity. However, due to the intimate link between glucose perception and metabolism, direct experimental proof for this hypothesis remained inconclusive. Still, our theoretical results provide a novel reason for the presence of low-affinity transport systems.

Indexed as

Biological TransportDiffusionKineticsMembrane Transport ProteinsModels, BiologicalSaccharomyces cerevisiae ProteinsMembrane Transport ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID29615663
PMCPMC5883050
OpenAlexW2801823793

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.