ArticleJournal of neuroendocrinology2012
Characterisation of human oestrogen receptor beta (ERβ) splice variants in neuronal cells.
Article in Journal of neuroendocrinology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- Estrogen Receptor Beta Isoforms Interplay Integrates Nuclear and Extra-Nuclear Signaling to Modulate Human Granulosa Cell Growth.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Estradiol Signaling at the Heart of Folliculogenesis: Its Potential Deregulation in Human Ovarian Pathologies.International journal of molecular sciences · 2022Review
- Promyelocytic Leukemia (PML) gene regulation: implication towards curbing oncogenesis.Cell death & disease · 2019Article
- Review
- Neuroanatomical and molecular correlates of cognitive and behavioural outcomes in hypogonadal males.Metabolic brain disease · 2018Review
- Structural and functional characteristics of oestrogen receptor β splice variants: Implications for the ageing brain.Journal of neuroendocrinology · 2018Review
- 17β-estradiol regulates the RNA-binding protein Nova1, which then regulates the alternative splicing of estrogen receptor β in the aging female rat brain.Neurobiology of aging · 2018Article
- Cooperation of Genomic and Rapid Nongenomic Actions of Estrogens in Synaptic Plasticity.Molecular neurobiology · 2017Review
- Phosphorylation Alters Oestrogen Receptor β-Mediated Transcription in Neurones.Journal of neuroendocrinology · 2015Article
- Prolonged ovarian hormone deprivation alters the effects of 17β-estradiol on microRNA expression in the aged female rat hypothalamus.Oncotarget · 2015Article
- Aging and Loss of Circulating 17β-Estradiol Alters the Alternative Splicing of ERβ in the Female Rat Brain.Endocrinology · 2015Article
- Age-dependent Effects of 17β-estradiol on the dynamics of estrogen receptor β (ERβ) protein-protein interactions in the ventral hippocampus.Molecular & cellular proteomics : MCP · 2014Article
- Estrogen: a master regulator of bioenergetic systems in the brain and body.Frontiers in neuroendocrinology · 2014Review
- Gender differences in neurodevelopment and epigenetics.Pflugers Archiv : European journal of physiology · 2013Review
- Estrogen signaling and the aging brain: context-dependent considerations for postmenopausal hormone therapy.ISRN endocrinology · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Oestrogen receptor (ER)α and ERβ are members of the ligand-activated superfamily of nuclear receptors and mediate most facets of oestrogen signalling. Several naturally occurring splice variants of each ER have been identified in the human brain, yet the biological significance of these splice variants in the brain remains unknown. In the present study, we exploit the unique structural differences of the human ERβ splice variants to determine the functional significance of individual ER domains in the brain. We previously established that full-length rodent ERβ (i.e. rERβ1) has constitutive transcriptional activity in neuronal cells in the absence of ligand. By contrast to the rodent splice variants, the human ERβ splice variants used in the present study contain varying length truncations of exon 8, which encodes for the E/F domains. Our results reveal that, in neuronal cells, each human-specific ERβ splice variant constitutively activated promoters mediated by a canonical oestrogen response element and repressed promoters mediated by activator protein-1 sites via p38 activity. From these data, we conclude that the C-terminus, encoding the AF-2 region and F domain, is not essential for the constitutive properties of human ERβ. Taken together, these studies show that human-specific ERβ variants are constitutively active and also provide novel insight into the contributions of the functional domains of ERβ towards mediating constitutive transcription at various promoters in neuronal cells.
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