Evidence map›Paper›PMID 25691753›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

RING finger protein 121 facilitates the degradation and membrane localization of voltage-gated sodium channels.

Kazutoyo Ogino, Sean E Low, Kenta Yamada, Louis Saint-Amant, Weibin Zhou, Akira Muto, Kazuhide Asakawa, Junichi Nakai, Koichi Kawakami, John Y Kuwada and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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
1.6field-weighted citation impact, top 19% 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, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Single-Cell Analysis of Rohon-Beard Neurons Implicates Fgf Signaling in Axon Maintenance and Cell Survival.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Characterization of zebrafish GABAScientific reports · 2021
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Defects of the Glycinergic Synapse in Zebrafish.Frontiers in molecular neuroscience · 2016
    Review
  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

11 authors at 6 institutions in 2 countries.

Kazutoyo OginoCenter for Frontier Research, National Institute of Genetics, Mishima 411-8540, Japan; Department of Chemistry and Biological Science, School of Science and Engineering, Aoyama Gakuin University, Sagamihara 252-5258, Japan;
Sean E LowHoward Hughes Medical Institute, The Rockefeller University, New York, NY 10065;
Kenta YamadaCenter for Frontier Research, National Institute of Genetics, Mishima 411-8540, Japan;
Louis Saint-AmantDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048;
Weibin ZhouDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048; Department of Pediatrics, University of Michigan Medical School, Ann Arbor, MI 48109-5646;
Akira MutoDivision of Molecular and Developmental Biology, National Institute of Genetics, Mishima 411-8540, Japan; Department of Genetics, Graduate University for Advanced Studies, Mishima 411-8540, Japan;
Kazuhide AsakawaDivision of Molecular and Developmental Biology, National Institute of Genetics, Mishima 411-8540, Japan; Department of Genetics, Graduate University for Advanced Studies, Mishima 411-8540, Japan;
Junichi NakaiSaitama University Brain Science Institute, Saitama 338-8570, Japan; and.
Koichi KawakamiDivision of Molecular and Developmental Biology, National Institute of Genetics, Mishima 411-8540, Japan; Department of Genetics, Graduate University for Advanced Studies, Mishima 411-8540, Japan;
John Y KuwadaDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048;
Hiromi HirataCenter for Frontier Research, National Institute of Genetics, Mishima 411-8540, Japan; Department of Chemistry and Biological Science, School of Science and Engineering, Aoyama Gakuin University, Sagamihara 252-5258, Japan; Department of Genetics, Graduate University for Advanced Studies, Mishima 411-8540, Japan; Precursory Research for Embryonic Science and Technology, Japan Science and Technology Agency, Saitama 332-0012, Japan hihirata@nig.ac.jp.
University of Michigan–Ann Arbor · USAoyama Gakuin University · JPNational Institute of Genetics · JPThe Graduate University for Advanced Studies, SOKENDAI · JPHoward Hughes Medical Institute · USSaitama University · JP

Funding

Genetic Analysis of Neuromuscular Junction FormationR01NS054731 · NINDS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KUWADA, JOHN Y · 2009 to 2012
$1.3M
Howard Hughes Medical InstituteNINDS NIH HHS R01 NS054731
6 · The paper itself

Abstract

Following their synthesis in the endoplasmic reticulum (ER), voltage-gated sodium channels (NaV) are transported to the membranes of excitable cells, where they often cluster, such as at the axon initial segment of neurons. Although the mechanisms by which NaV channels form and maintain clusters have been extensively examined, the processes that govern their transport and degradation have received less attention. Our entry into the study of these processes began with the isolation of a new allele of the zebrafish mutant alligator, which we found to be caused by mutations in the gene encoding really interesting new gene (RING) finger protein 121 (RNF121), an E3-ubiquitin ligase present in the ER and cis-Golgi compartments. Here we demonstrate that RNF121 facilitates two opposing fates of NaV channels: (i) ubiquitin-mediated proteasome degradation and (ii) membrane localization when coexpressed with auxiliary NaVβ subunits. Collectively, these results indicate that RNF121 participates in the quality control of NaV channels during their synthesis and subsequent transport to the membrane.

Indexed as

ProteolysisRING Finger DomainsAnimalsBase SequenceCell MembraneMolecular Sequence DataMutationProteasome Endopeptidase ComplexProtein TransportUbiquitinUbiquitin-Protein LigasesVoltage-Gated Sodium ChannelsZebrafishZebrafish ProteinsProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesVoltage-Gated Sodium ChannelsZebrafish Proteinsescapetouch responseubiquitinvoltage-gated sodium channelzebrafish

Identifiers

PMID25691753
PMCPMC4352840
OpenAlexW2068380982

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.