ArticleBMC molecular biology2010
Functional and cellular characterization of human Retinoic Acid Induced 1 (RAI1) mutations associated with Smith-Magenis Syndrome.
Article in BMC molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 42 citations in OpenAlex.
- CRISPR screening identifies TRIM27 as a destabilizer of the Smith-Magenis syndrome protein RAI1.Genetics · 2026Article
- Rare Variant Analyses in Ancestrally Diverse Cohorts Reveal Novel ADHD Risk Genes.medRxiv : the preprint server for health sciences · 2025Article
- Whole Exome Sequencing of a Multiplex Family of Indian Origin Identifies Variants in theMolecular syndromology · 2024Article
- NovelJournal of personalized medicine · 2024Article
- A case of Smith-Magenis syndrome with skin manifestations caused by a novel locus mutation in the RAI1 gene.The Journal of international medical research · 2023Article
- Retinoic acid-induced 1 gene haploinsufficiency alters lipid metabolism and causes autophagy defects in Smith-Magenis syndrome.Cell death & disease · 2022Article
- Review
- The role of the retinoids in schizophrenia: genomic and clinical perspectives.Molecular psychiatry · 2020Review
- A Rare De NovoBiology · 2018Article
- Article
- Review
- GENETIC AND EPIGENETIC CAUSES OF OBESITY.Adolescent medicine: state of the art reviews · 2017Review
- Evidence for genetic regulation of mRNA expression of the dosage-sensitive gene retinoic acid induced-1 (RAI1) in human brain.Scientific reports · 2016Article
- Article
- Whole exome sequencing identifies RAI1 mutation in a morbidly obese child diagnosed with ROHHAD syndrome.The Journal of clinical endocrinology and metabolism · 2015Article
- Expression in the human brain of retinoic acid induced 1, a protein associated with neurobehavioural disorders.Brain structure & function · 2015Article
- Increased expression of retinoic acid-induced gene 1 in the dorsolateral prefrontal cortex in schizophrenia, bipolar disorder, and major depression.Neuropsychiatric disease and treatment · 2015Article
- Identification of Nine New RAI1-Truncating Mutations in Smith-Magenis Syndrome Patients without 17p11.2 Deletions.Molecular syndromology · 2014Article
- Detection of classical 17p11.2 deletions, an atypical deletion and RAI1 alterations in patients with features suggestive of Smith-Magenis syndrome.European journal of human genetics : EJHG · 2012Article
- RAI1 transcription factor activity is impaired in mutants associated with Smith-Magenis Syndrome.PloS one · 2012Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundSmith-Magenis Syndrome is a contiguous gene syndrome in which the dosage sensitive gene has been identified: the Retinoic Acid Induced 1 (RAI1). Little is known about the function of human RAI1.
resultsWe generated the full-length cDNA of the wild type protein and five mutated forms: RAI1-HA 2687delC, RAI1-HA 3103delC, RAI1 R960X, RAI1-HA Q1562R, and RAI1-HA S1808N. Four of them have been previously associated with SMS clinical phenotype. Molecular weight, subcellular localization and transcription factor activity of the wild type and mutant forms were studied by western blot, immunofluorescence and luciferase assays respectively. The wild type protein and the two missense mutations presented a higher molecular weight than expected, localized to the nucleus and activated transcription of a reporter gene. The frameshift mutations generated a truncated polypeptide with transcription factor activity but abnormal subcellular localization, and the same was true for the 1-960aa N-terminal half of RAI1. Two different C-terminal halves of the RAI1 protein (1038aa-end and 1229aa-end) were able to localize into the nucleus but had no transactivation activity.
conclusionOur results indicate that transcription factor activity and subcellular localization signals reside in two separate domains of the protein and both are essential for the correct functionality of RAI1. The pathogenic outcome of some of the mutated forms can be explained by the dissociation of these two domains.
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