Evidence map›Paper›PMID 35876901›Full record

ArticleCellular and molecular life sciences : CMLS2022

Retinoschisin and novel Na/K-ATPase interaction partners Kv2.1 and Kv8.2 define a growing protein complex at the inner segments of mammalian photoreceptors.

Verena Schmid, Alexander Wurzel, Christian H Wetzel, Karolina Plössl, Astrid Bruckmann, Patricia Luckner, Bernhard H F Weber, Ulrike Friedrich

Open access · hybridAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Cells · 2025
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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

8 authors at 2 institutions in 1 country.

Verena SchmidInstitute of Human Genetics, University of Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg, Germany.
Alexander WurzelInstitute of Human Genetics, University of Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg, Germany.
Christian H WetzelDepartment of Psychiatry and Psychotherapy, University of Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg, Germany.
Karolina PlösslInstitute of Human Genetics, University of Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg, Germany.
Astrid BruckmannInstitute of Biochemistry, Genetics and Microbiology, Protein Mass Spectrometry Group, University of Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Patricia LucknerInstitute of Biochemistry, Genetics and Microbiology, Protein Mass Spectrometry Group, University of Regensburg, Universitätsstraße 31, 93053, Regensburg, Germany.
Bernhard H F WeberInstitute of Human Genetics, University of Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg, Germany. bweb@klinik.uni-regensburg.de.ORCID http://orcid.org/0000-0002-8808-7723
Ulrike FriedrichInstitute of Human Genetics, University of Regensburg, Franz-Josef-Strauss-Allee 11, 93053, Regensburg, Germany. ulrike.friedrich@klinik.uni-regensburg.de.
University of Regensburg · DEUniversity Hospital Regensburg · DE

Funding

Deutsche Forschungsgemeinschaft 91b GGDeutsche Forschungsgemeinschaft FR 3377/1-2Deutsche Forschungsgemeinschaft INST 89/506-1 FUGGDeutsche Forschungsgemeinschaft Project Z1Deutsche Forschungsgemeinschaft SFB 960
6 · The paper itself

Abstract

The RS1 gene on Xp 22.13 encodes retinoschisin which is known to directly interact with the retinal Na/K-ATPase at the photoreceptor inner segments. Pathologic mutations in RS1 cause X-linked juvenile retinoschisis (XLRS), a hereditary retinal dystrophy in young males. To further delineate the retinoschisin-Na/K-ATPase complex, co-immunoprecipitation was performed with porcine and murine retinal lysates targeting the ATP1A3 subunit. This identified the voltage-gated potassium (Kv) channel subunits Kv2.1 and Kv8.2 as direct interaction partners of the retinal Na/K-ATPase. Colocalization of the individual components of the complex was demonstrated at the membrane of photoreceptor inner segments. We further show that retinoschisin-deficiency, a frequent consequence of molecular pathology in XLRS, causes mislocalization of the macromolecular complex during postnatal retinal development with a simultaneous reduction of Kv2.1 and Kv8.2 protein expression, while the level of retinal Na/K-ATPase expression remains unaffected. Patch-clamp analysis revealed no effect of retinoschisin-deficiency on Kv channel mediated potassium ion currents in vitro. Together, our data suggest that Kv2.1 and Kv8.2 together with retinoschisin and the retinal Na/K-ATPase are integral parts of a macromolecular complex at the photoreceptor inner segments. Defective compartmentalization of this complex due to retinoschisin-deficiency may be a crucial step in initial XLRS pathogenesis.

Indexed as

Eye ProteinsRetinoschisisAnimalsMaleMammalsMicePhotoreceptor CellsPotassiumSodium-Potassium-Exchanging ATPaseSwineAtp1a3 protein, mouseEye ProteinsPotassiumSodium-Potassium-Exchanging ATPaseKv2.1Kv8.2Retinal Na/K-ATPaseRetinoschisinRS1Voltage-gated potassium channelX-linked juvenile retinoschisis

Identifiers

PMID35876901
PMCPMC9314279
OpenAlexW4287447086

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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 Socratic graph.