Research summary
Retinoid signalling is reviewed through the lens of ligand-activated nuclear receptors, identifying two retinoid-receptor families — RARα/β/γ (activated by all-trans and 9-cis retinoic acid) and RXRα/β/γ (activated by 9-cis retinoic acid) — and the multiple isoforms each generates through differential promoter usage and alternative splicing of the 5' UTR; the receptors heterodimerize as RAR-RXR pairs (and RXR also pairs with other nuclear receptors) and bind retinoic acid response elements with characteristic direct-repeat spacing to control transcription. Combinatorial complexity at the level of ligand, receptor isoform, dimerisation partner, coregulator recruitment, and target gene contributes to the pleiotropic developmental and homeostatic effects of retinoic acid across embryonic patterning, organogenesis, epithelial differentiation, and metabolism [2]. A functional study of estrogen-receptor (ER) regulation identifies Ser118 as a phosphorylation site required for full activity of ER's AF-1 activation function; Ser118 is phosphorylated by mitogen-activated protein kinase (MAPK) in vitro and after EGF or IGF stimulation in cells, and overexpression of MAPK kinase (MAPKK) or of the guanine-nucleotide-binding protein Ras (both of which activate MAPK) enhances both estrogen- and tamoxifen-induced transcriptional activity of wild-type ER but not of an ER Ser118-to-Ala mutant. The amino-terminal AF-1 of ER is therefore modulated by growth-factor-driven kinase cascades, providing a mechanism for ligand-independent or ligand-augmented activation of the receptor in tissues exposed to mitogenic signalling, with direct implications for tamoxifen pharmacology in MAPK-active breast tumours [3]. A broader review of split-gene organization frames how interrupted (intron-containing) eukaryotic genes coding for proteins are transcribed by RNA polymerase II, processed through splicing and polyadenylation, and expressed, situating retinoid and steroid-receptor signalling within the larger context of regulated transcription from interrupted gene architectures and the recognition that gene structure itself contributes to expression diversity [1].
Recent publications
- The nuclear receptor superfamily: The second decadeDOI
- Organization and Expression of Eucaryotic Split Genes Coding for ProteinsDOI
- A decade of molecular biology of retinoic acid receptorsDOI
- Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-ADOI
- A human retinoic acid receptor which belongs to the family of nuclear receptorsDOI
- Activation of the Estrogen Receptor Through Phosphorylation by Mitogen-Activated Protein KinaseDOI
- Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B.DOI
- Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficientlyDOI
- Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-αDOI
- In vivo sequence requirements of the SV40 early promoter regionDOI
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External profiles
- ORCID: https://orcid.org/0000-0002-7861-6046
- OpenAlex: openalex.org
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