Evidence map›Paper›PMID 31036257›Full record

ArticleBiophysical journal2019

Engineered Passive Potassium Conductance in the KR2 Sodium Pump.

Arend Vogt, Arita Silapetere, Christiane Grimm, Florian Heiser, Maximiliano Ancina Möller, Peter Hegemann

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.7field-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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. NaMolecules (Basel, Switzerland) · 2023
    Review
  3. Article
  4. KInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  9. Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  10. Structure-Function Relationship of Channelrhodopsins.Advances in experimental medicine and biology · 2021
    Review
  11. Article
  12. Optogenetic Modulation of Ion Channels by Photoreceptive Proteins.Advances in experimental medicine and biology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
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 1 institution in 1 country.

Arend VogtInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.
Arita SilapetereInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.
Christiane GrimmInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.
Florian HeiserInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.
Maximiliano Ancina MöllerInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany.
Peter HegemannInstitute of Biology, Experimental Biophysics, Humboldt-Universität zu Berlin, Berlin, Germany. Electronic address: hegemann@rz.hu-berlin.de.
Humboldt-Universität zu Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Light-driven sodium pumps (NaRs) are microbial rhodopsins that utilize light energy to actively transport sodium ions out of the cell. Here, we used targeted mutagenesis and electrophysiological methods in living cells to demonstrate that NaRs can be converted into light-activated cation channels by molecular engineering. Specifically, introduction of the R109Q mutation into the sodium ion pump of Dokdonia eikasta (KR2) results in passive ion conductance, with a high preference for potassium over sodium ions. However, in this mutant, residual active outward pumping of sodium ions competes with passive inward transport of potassium. Channel-like behavior could also be achieved by introduction of other mutations into the KR2 counterion complex, and further, these modifications were transferrable to other NaRs. Combining the R109Q replacement with modifications at position S70 removed the residual sodium pumping and greatly enhanced the channel-like activity. However, passive photocurrents were only observed in leak mutants if the KR2 counterions, D116 and D251, were deprotonated, which was only observed under alkaline conditions. Overall, our results reveal that interactions between R109 and the nearby residues, L75, S70, D116, and D251, prevent passive backflow during ion transport in NaRs.

Indexed as

AnimalsBiological TransportCell LineCell MembraneEscherichia coliFlavobacteriaceaeHydrogen-Ion ConcentrationIon TransportLightMiceMutant ProteinsPotassiumProtein BindingProtein ConformationRatsRhodopsins, MicrobialMutant ProteinsPotassiumRhodopsins, MicrobialSodiumSodium-Potassium-Exchanging ATPase

Identifiers

PMID31036257
PMCPMC6531830
OpenAlexW2939571633

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.