Evidence map›Paper›PMID 26530008›Full record

ArticleScientific reports2015

Neuromuscular regulation in zebrafish by a large AAA+ ATPase/ubiquitin ligase, mysterin/RNF213.

Yuri Kotani, Daisuke Morito, Satoru Yamazaki, Kazutoyo Ogino, Koichi Kawakami, Seiji Takashima, Hiromi Hirata, Kazuhiro Nagata

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

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  5. RNF213 loss of function reshapes vascular transcriptome and spliceosome leading to disrupted angiogenesis and aggravated vascular inflammatory responses.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2022
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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 6 institutions in 1 country.

Yuri KotaniLaboratory of Molecular and Cellular Biology, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 606-8397, Japan.
Daisuke MoritoLaboratory of Molecular and Cellular Biology, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 606-8397, Japan.
Satoru YamazakiDepartment of Cell Biology, National Cerebral and Cardiovascular Center, Suita 565-8565, Japan.
Kazutoyo OginoDepartment of Chemistry and Biological Science, School of Science and Engineering, Aoyama Gakuin University, Sagamihara 252-5258, Japan.
Koichi KawakamiDivision of Molecular and Developmental Biology, National Institute of Genetics and Department of Genetics, Sokendai (The Graduate University for Advanced Studies), Mishima 411-8540, Japan.
Seiji TakashimaDepartment of Medical Biochemistry, Graduate School of Medicine, Osaka University, Suita 565-0871, Japan.
Hiromi HirataDepartment of Chemistry and Biological Science, School of Science and Engineering, Aoyama Gakuin University, Sagamihara 252-5258, Japan.
Kazuhiro NagataLaboratory of Molecular and Cellular Biology, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto 606-8397, Japan.
Kyoto Sangyo University · JPNational Institute of Genetics · JPAoyama Gakuin University · JPJapan Science and Technology Agency · JPNational Cerebral and Cardiovascular Center · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mysterin (also known as RNF213) is a huge intracellular protein with two AAA+ ATPase modules and a RING finger ubiquitin ligase domain. Mysterin was originally isolated as a significant risk factor for the cryptogenic cerebrovascular disorder moyamoya disease, and was found to be involved in physiological angiogenesis in zebrafish. However, the function and the physiological significance of mysterin in other than blood vessels remain largely unknown, although mysterin is ubiquitously expressed in animal tissues. In this study, we performed antisense-mediated suppression of a mysterin orthologue in zebrafish larvae and revealed that mysterin-deficient larvae showed significant reduction in fast myofibrils and immature projection of primary motoneurons, leading to severe motor deficits. Fast muscle-specific restoration of mysterin expression cancelled these phenotypes, and interestingly both AAA+ ATPase and ubiquitin ligase activities of mysterin were indispensable for proper fast muscle formation, demonstrating an essential role of mysterin and its enzymatic activities in the neuromuscular regulation in zebrafish.

Indexed as

AnimalsAnimals, Genetically ModifiedHumansImmunohistochemistryLarvaMicroscopy, ElectronMotor ActivityMotor NeuronsMuscle Fibers, SkeletalNeovascularization, PhysiologicOligonucleotides, AntisenseRING Finger DomainsUbiquitin-Protein LigasesZebrafishZebrafish ProteinsOligonucleotides, AntisenseUbiquitin-Protein LigasesZebrafish Proteins

Identifiers

PMID26530008
PMCPMC4632019
OpenAlexW2406842129

What OpenQuestion holds

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LicenceCC BY
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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.