Evidence map›Paper›PMID 33953269›Full record

ArticleScientific reports2021

A novel RLIM/RNF12 variant disrupts protein stability and function to cause severe Tonne-Kalscheuer syndrome.

Francisco Bustos, Carmen Espejo-Serrano, Anna Segarra-Fas, Rachel Toth, Alison J Eaton, Kristin D Kernohan, Meredith J Wilson, Lisa G Riley, Greg M Findlay

Open access · goldAbstract readCase Reports
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

9 citing papers in PubMed, 11 citations in OpenAlex.

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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

9 authors at 6 institutions in 3 countries.

Francisco Bustos *MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Carmen Espejo-Serrano *MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Anna Segarra-Fas *MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Rachel TothMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Alison J EatonDepartment of Medical Genetics, University of Alberta, Edmonton, AB, Canada.
Kristin D KernohanNewborn Screening Ontario, Children's Hospital of Eastern Ontario, Ottawa, Canada.
Meredith J WilsonDepartment of Clinical Genetics, The Children's Hospital at Westmead, Sydney, Australia.
Lisa G RileyRare Diseases Functional Genomics, Kids Research, The Children's Hospital at Westmead and The Children's Medical Research Institute, Sydney, Australia. lisa.riley@health.nsw.gov.au.
Greg M FindlayMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK. g.m.findlay@dundee.ac.uk.
University of Dundee · GBChildren's Hospital at Westmead · AUMRC Protein Phosphorylation and Ubiquitylation Unit · GBUniversity of Alberta · CAUniversity of Ottawa · CAUniversity of Sydney · AU

Funding

Medical Research Council MR/N000609/1Wellcome TrustWellcome Trust 211209/Z/18/Z
6 · The paper itself

Abstract

Tonne-Kalscheuer syndrome (TOKAS) is an X-linked intellectual disability syndrome associated with variable clinical features including craniofacial abnormalities, hypogenitalism and diaphragmatic hernia. TOKAS is caused exclusively by variants in the gene encoding the E3 ubiquitin ligase gene RLIM, also known as RNF12. Here we report identification of a novel RLIM missense variant, c.1262A>G p.(Tyr421Cys) adjacent to the regulatory basic region, which causes a severe form of TOKAS resulting in perinatal lethality by diaphragmatic hernia. Inheritance and X-chromosome inactivation patterns implicate RLIM p.(Tyr421Cys) as the likely pathogenic variant in the affected individual and within the kindred. We show that the RLIM p.(Tyr421Cys) variant disrupts both expression and function of the protein in an embryonic stem cell model. RLIM p.(Tyr421Cys) is correctly localised to the nucleus, but is readily degraded by the proteasome. The RLIM p.(Tyr421Cys) variant also displays significantly impaired E3 ubiquitin ligase activity, which interferes with RLIM function in Xist long-non-coding RNA induction that initiates imprinted X-chromosome inactivation. Our data uncover a highly disruptive missense variant in RLIM that causes a severe form of TOKAS, thereby expanding our understanding of the molecular and phenotypic spectrum of disease severity.

Indexed as

Craniofacial AbnormalitiesHernia, DiaphragmaticHypogonadismIntellectual DisabilityMutation, MissenseUbiquitin-Protein LigasesHumansInfant, NewbornMaleUbiquitinationRLIM protein, humanUbiquitin-Protein Ligases

Identifiers

PMID33953269
PMCPMC8100121
OpenAlexW3158870224

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.