Evidence map›Paper›PMID 26781468›Full record

ArticleCellular and molecular life sciences : CMLS2016

The function of the two-pore channel TPC1 depends on dimerization of its carboxy-terminal helix.

Nina Larisch, Sonja A Kirsch, Alexandra Schambony, Tanja Studtrucker, Rainer A Böckmann, Petra Dietrich

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2016. 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
4.9field-weighted citation impact, top 5% 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. Article
  2. Review
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  6. Voltage-gating and cytosolic CaProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Endolysosomal CaCancers · 2018
    Review
  9. Article
  10. Structural basis for activation of voltage sensor domains in an ion channel TPC1.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Review
  14. Article
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  16. 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 1 institution in 1 country.

Nina LarischMolecular Plant Physiology, Department of Biology, University of Erlangen-Nürnberg, Staudtstrasse 5, 91058, Erlangen, Germany.
Sonja A KirschComputational Biology, Department of Biology, University of Erlangen-Nürnberg, Staudtstrasse 5, 91058, Erlangen, Germany.
Alexandra SchambonyDevelopmental Biology, Department of Biology, University of Erlangen-Nürnberg, Staudtstrasse 5, 91058, Erlangen, Germany.
Tanja StudtruckerMolecular Plant Physiology, Department of Biology, University of Erlangen-Nürnberg, Staudtstrasse 5, 91058, Erlangen, Germany.
Rainer A BöckmannComputational Biology, Department of Biology, University of Erlangen-Nürnberg, Staudtstrasse 5, 91058, Erlangen, Germany.
Petra DietrichMolecular Plant Physiology, Department of Biology, University of Erlangen-Nürnberg, Staudtstrasse 5, 91058, Erlangen, Germany. petra.dietrich@fau.de.ORCID 0000-0002-9209-8089
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two-pore channels (TPCs) constitute a family of intracellular cation channels with diverse permeation properties and functions in animals and plants. In the model plant Arabidopsis, the vacuolar cation channel TPC1 is involved in propagation of calcium waves and in cation homeostasis. Here, we discovered that the dimerization of a predicted helix within the carboxyl-terminus (CTH) is essential for the activity of TPC1. Bimolecular fluorescence complementation and co-immunoprecipitation demonstrated the interaction of the two C-termini and pointed towards the involvement of the CTH in this process. Synthetic CTH peptides dimerized with a dissociation constant of 3.9 µM. Disruption of this domain in TPC1 either by deletion or point mutations impeded the dimerization and cation transport. The homo-dimerization of the CTH was analyzed in silico using coarse-grained molecular dynamics (MD) simulations for the study of aggregation, followed by atomistic MD simulations. The simulations revealed that the helical region of the wild type, but not a mutated CTH forms a highly stable, antiparallel dimer with characteristics of a coiled-coil. We propose that the voltage- and Ca(2+)-sensitive conformation of TPC1 depends on C-terminal dimerization, adding an additional layer to the complex regulation of two-pore cation channels.

Indexed as

Calcium SignalingArabidopsisArabidopsis ProteinsCalcium ChannelsHEK293 CellsHumansMolecular Dynamics SimulationPoint MutationProtein Conformation, alpha-HelicalProtein MultimerizationTwo-Pore ChannelsArabidopsis ProteinsCalcium ChannelsTPC1 protein, ArabidopsisTwo-Pore ChannelsCalcium signalingMD simulationMicroscale thermophoresisMutationPatch-clampVacuole

Identifiers

PMID26781468
PMCPMC4894940
OpenAlexW2273960951

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.