Evidence map›Paper›PMID 33059680›Full record

ArticleBMC biology2020

The mono-ADP-ribosyltransferase ARTD10 regulates the voltage-gated K

Yuemin Tian, Patricia Korn, Priyanka Tripathi, Daniel Komnig, Dominik Wiemuth, Azadeh Nikouee, Arno Classen, Carsten Bolm, Björn H Falkenburger, Bernhard Lüscher and 1 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Intracellular mono-ADP-ribosyltransferases at the host-virus interphase.Cellular and molecular life sciences : CMLS · 2022
    Review
  5. Article
  6. 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

11 authors at 2 institutions in 1 country.

Yuemin TianInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Patricia KornInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Priyanka TripathiInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Daniel KomnigDepartment of Neurology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Dominik WiemuthInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Azadeh NikoueeInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Arno ClassenInstitute of Organic Chemistry, RWTH Aachen University, Landoltweg 1, 52056, Aachen, Germany.
Carsten BolmInstitute of Organic Chemistry, RWTH Aachen University, Landoltweg 1, 52056, Aachen, Germany.
Björn H FalkenburgerDepartment of Neurology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Bernhard LüscherInstitute of Biochemistry and Molecular Biology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany.
Stefan GründerInstitute of Physiology, RWTH Aachen University, Pauwelsstrasse 30, 52074, Aachen, Germany. sgruender@ukaachen.de.ORCID 0000-0002-7635-9883
RWTH Aachen University · DEForschungszentrum Jülich · DE

Funding

Deutsche Forschungsgemeinschaft LU466/16-2Deutsche Forschungsgemeinschaft VE1093/1-1
6 · The paper itself

Abstract

backgroundADP-ribosylation is a ubiquitous post-translational modification that involves both mono- and poly-ADP-ribosylation. ARTD10, also known as PARP10, mediates mono-ADP-ribosylation (MARylation) of substrate proteins. A previous screen identified protein kinase C delta (PKCδ) as a potential ARTD10 substrate, among several other kinases. The voltage-gated K

resultsWe found that ARTD10 inhibited PKCδ, which increased Kv1.1 current amplitude and the proportion of the inactivating current component in HeLa cells, indicating that ARTD10 regulates Kv1.1 in living cells. An inhibitor of ARTD10, OUL35, significantly decreased peak amplitude together with the proportion of the inactivating current component of Kv1.1-containing channels in primary hippocampal neurons, demonstrating that the ARTD10-PKCδ signaling cascade regulates native Kv1.1. Moreover, we show that the pharmacological blockade of ARTD10 increases excitability of hippocampal neurons.

conclusionsOur results, for the first time, suggest that MARylation by ARTD10 controls neuronal excitability.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAnimalsHEK293 CellsHeLa CellsHumansKv1.1 Potassium ChannelMicePoly(ADP-ribose) PolymerasesProtein Kinase C-deltaProto-Oncogene ProteinsKCNA1 protein, humanKv1.1 Potassium ChannelPARP10 protein, humanPoly(ADP-ribose) PolymerasesPRKCD protein, humanProtein Kinase C-deltaProto-Oncogene ProteinsADP ribosylationADP ribosyltransferaseIon channelPARP10Posttranslational modificationPotassium channelProtein kinase C delta

Identifiers

PMID33059680
PMCPMC7558731
OpenAlexW3093321808

What OpenQuestion holds

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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.