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OXR1A, a Coactivator of PRMT5 Regulating Histone Arginine Methylation

Yang, Mingyi ; Lin, Xiaolin ; Segers, Filip ; Suganthan, Rajikala ; Hildrestrand, Gunn A. ; Rinholm, Johanne E. ; Aas, Per Arne ; Sousa, Mirta M.L. ; Holm, Sverre ; Bolstad, Nils ; Warren, David ; Berge, Rolf K. ; Johansen, Rune F. ; Yndestad, Arne ; Kristiansen, Elise ; Klungland, Arne ; Luna, Luisa ; Eide, Lars ; Halvorsen, Bente ; Aukrust, Pål ; Bjørås, Magnar

Cell reports (Cambridge), 2020-03, Vol.30 (12), p.4165-4178.e7 [Periódico revisado por pares]

United States: Elsevier Inc

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Título:
OXR1A, a Coactivator of PRMT5 Regulating Histone Arginine Methylation
Autor: Yang, Mingyi ; Lin, Xiaolin ; Segers, Filip ; Suganthan, Rajikala ; Hildrestrand, Gunn A. ; Rinholm, Johanne E. ; Aas, Per Arne ; Sousa, Mirta M.L. ; Holm, Sverre ; Bolstad, Nils ; Warren, David ; Berge, Rolf K. ; Johansen, Rune F. ; Yndestad, Arne ; Kristiansen, Elise ; Klungland, Arne ; Luna, Luisa ; Eide, Lars ; Halvorsen, Bente ; Aukrust, Pål ; Bjørås, Magnar
Assuntos: Animals ; Arginine - metabolism ; Arginine Methylation ; Brain - metabolism ; brain-liver axis ; Cell Line ; epigenetic regulation ; Fatty Liver - genetics ; Fatty Liver - pathology ; Female ; Gene Expression Regulation ; Growth hormone ; Growth Hormone - blood ; Growth Hormone - metabolism ; H3R2me2s ; Histones - metabolism ; Hormones - metabolism ; Immunity - genetics ; Liver - metabolism ; Liver - pathology ; Male ; Methylation ; Mice, Inbred C57BL ; Mice, Knockout ; Mitochondrial Proteins - chemistry ; Mitochondrial Proteins - deficiency ; Mitochondrial Proteins - metabolism ; NAFLD ; neuroendocrine regulation ; Non-alcoholic fatty liver disease ; Organ Specificity ; Oxidation resistance gene 1 ; OXR1 ; pituitary gland ; Pituitary Gland - metabolism ; PRMT1 ; PRMT5 ; Promoter Regions, Genetic - genetics ; protein arginine methyltransferase ; Protein Binding ; Protein Domains ; Protein-Arginine N-Methyltransferases - metabolism ; Rats ; Receptors, Somatotropin - metabolism ; STAT5 Transcription Factor - metabolism ; Structure-Activity Relationship ; Transcriptome - genetics
É parte de: Cell reports (Cambridge), 2020-03, Vol.30 (12), p.4165-4178.e7
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
NFR/240099/F20
Descrição: Oxidation resistance gene 1 (OXR1) protects cells against oxidative stress. We find that male mice with brain-specific isoform A knockout (Oxr1A−/−) develop fatty liver. RNA sequencing of male Oxr1A−/− liver indicates decreased growth hormone (GH) signaling, which is known to affect liver metabolism. Indeed, Gh expression is reduced in male mice Oxr1A−/− pituitary gland and in rat Oxr1A−/− pituitary adenoma cell-line GH3. Oxr1A−/− male mice show reduced fasting-blood GH levels. Pull-down and proximity ligation assays reveal that OXR1A is associated with arginine methyl transferase PRMT5. OXR1A-depleted GH3 cells show reduced symmetrical dimethylation of histone H3 arginine 2 (H3R2me2s), a product of PRMT5 catalyzed methylation, and chromatin immunoprecipitation (ChIP) of H3R2me2s shows reduced Gh promoter enrichment. Finally, we demonstrate with purified proteins that OXR1A stimulates PRMT5/MEP50-catalyzed H3R2me2s. Our data suggest that OXR1A is a coactivator of PRMT5, regulating histone arginine methylation and thereby GH production within the pituitary gland. [Display omitted] •OXR1A interacts with histone arginine methyltransferase PRMT5•OXR1A stimulates PRMT5/MEP50-mediated H3 methylation in vitro•OXR1A promotes GH expression in pituitary via H3R2 symmetric demethylation•Depletion of Oxr1A results in GH deficiency and fatty liver in adult male mice Yang et al. show that OXR1A interacts with methyltransferase PRMT5 to promote arginine methylation of histone H3R2 and to regulate transcription of growth hormone in the pituitary gland. Male mice with OXR1A knockout display growth-hormone deficiency and develop fatty liver.
Editor: United States: Elsevier Inc
Idioma: Inglês;Norueguês

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OXR1A, a Coactivator of PRMT5 Regulating Histone Arginine Methylation

United States: Elsevier Inc

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