ArticleStem cells (Dayton, Ohio)2016
Retinoic Acid Induces Ubiquitination-Resistant RIP140/LSD1 Complex to Fine-Tune Pax6 Gene in Neuronal Differentiation.
Article in Stem cells (Dayton, Ohio), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- A role for the transcriptional coregulator RIP140 in the control of muscle endurance fitness.JCI insight · 2025Article
- The multifaceted role of post-translational modifications of LSD1 in cellular processes and disease pathogenesis.Genes & diseases · 2025Review
- Review
- Article
- All-International journal of molecular sciences · 2019Review
- Receptor-interacting protein 140 as a co-repressor of Heat Shock Factor 1 regulates neuronal stress response.Cell death & disease · 2017Article
- Combination of RNA Interference and Stem Cells for Treatment of Central Nervous System Diseases.Genes · 2017Review
- Correlation between receptor-interacting protein 140 expression and directed differentiation of human embryonic stem cells into neural stem cells.Neural regeneration research · 2017Article
- The Stagnant Adaptation of Defined and Xeno-Free Culture of iPSCs in Academia.Archives of stem cell research · 2015Article
- Identification of neuron-related genes for cell therapy of neurological disorders by network analysis.Journal of Zhejiang University. Science. BArticle
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Receptor-interacting protein 140 (RIP140) is a wide-spectrum coregulator for hormonal regulation of gene expression, but its activity in development/stem cell differentiation is unknown. Here, we identify RIP140 as an immediate retinoic acid (RA)-induced dual-function chaperone for LSD1 (lysine-specific demethylase 1). RIP140 protects LSD1's catalytic domain and antagonizes its Jade-2-mediated ubiquitination and degradation. In RA-induced neuronal differentiation, the increased RIP140/LSD1 complex is recruited by RA-elevated Pit-1 to specifically reduce H3K4me2 modification on the Pax6 promoter, thereby repressing RA-induction of Pax6. This study reveals a new RA-induced gene repressive mechanism that modulates the abundance, enzyme quality, and recruitment of histone modifier LSD1 to neuronal regulator Pax6, which provides a homeostatic control for RA induction of neuronal differentiation.
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