JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer
Open accessAbstract
Histone methylation is a dynamic process that participates in a diverse array of cellular processes and has been found to associate with cancer. Recently, several histone demethylases have been identified that catalyze the removal of methylation from histone H3 lysine residues. Through bioinformatic and biochemical analysis, we identified JARID1B as a H3K4 demethylase. Overexpression of JARID1B resulted in loss of tri-, di-, and monomethyl H3K4 but did not affect other histone lysine methylations. In vitro biochemical experiments demonstrated that JARID1B directly catalyzes the demethylation. The enzymatic activity requires the JmjC domain and uses Fe(II) and α-ketoglutarate as cofactors. Furthermore, we found that JARID1B is up-regulated in prostate cancer tissues, compared with benign prostate samples. We also demonstrated that JARID1B associates with androgen receptor and regulates its transcriptional activity. Thus, we identified JARID1B as a demethylase capable of removing three methyl groups from histone H3 lysine 4 and up-regulated in prostate cancer.
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The authors identified four dURVs in schizophrenia cases and none in controls in KDM5C, 11 in cases and 2 in controls in KDM5B, and 11 in cases and 3 in controls in ITPR1.
“we identified four dURVs in schizophrenia cases (and none in controls) in XLID gene KDM5C, an H3K4 methylation eraser gene44, 11 dURVs in cases (and 2 in controls) in DD gene KDM5B, another H3K4 methylation eraser gene45, and 11 dURVs in cases (and 3 in controls) in DD gene ITPR1, which encodes an inositol triphosphate receptor46 (Supplementary Tables 2 and 3).”
From Increased burden of ultra-rare protein-altering variants among 4,877 individuals with schizophrenia (2016) · cites this paper as [45]
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- Authors
- Xiang, Y., Zhu, Z., Han, G., Ye, X., Xu, B., Peng, Z., Ma, Y., Yu, Y., Lin, H., Chen, A. P., & Chen, C. D.
- Affiliations
- Chinese Academy of Sciences (CN)
- Center for Excellence in Molecular Cell Science (CN)
- University of California San Diego (US)
- Corresponding author
- Chen, Adele Pin
- Chen, Charlie Degui
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2007-12-04
- Volume
- 104
- Issue
- 49
- Pages
- 19226-19231
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2148272
- OpenAlex
- W2090805227
- Cited by
- 395
- References
- 37
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 16 · 2023: 20 · 2022: 20 · 2021: 28 · 2020: 16 · 2019: 14 · 2018: 28 · 2017: 18 · 2016: 23 · 2015: 34 · 2014: 25 · 2013: 26 · 2012: 28
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Memorial Sloan-Kettering Cancer Center
- Cancer Research UK
- Chinese Academy of Sciences (KSCX2-YW-R)
- National Key Research and Development Program of China (2007CB947100, 2007CB947900)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
- Keywords
- JARID1B, H3K4 demethylation, prostate cancer, histone methylation, JmjC domain, alpha-ketoglutarate, iron cofactor, androgen receptor, transcriptional regulation, protein overexpression
- MeSH terms
- DNA-Binding Proteins, Histones, Humans, Lysine, Male, Methylation, Nuclear Proteins, Phylogeny, Prostatic Neoplasms, Repressor Proteins, Up-Regulation, Gene Expression, Protein Structure, Tertiary, Computational Biology, Cell Line, Tumor, Dioxygenases, Jumonji Domain-Containing Histone Demethylases
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