p300-mediated acetylation of histone demethylase JMJD1A prevents its degradation by ubiquitin ligase STUB1 and enhances its activity in prostate cancer
Open accessAbstract
The androgen receptor (AR) pathway plays a central role in the development of castration-resistant prostate cancer (CRPC). The histone demethylase JMJD1A has been shown to regulate activities of AR and c-Myc transcription factors and promote prostate cancer progression. Here, we report that JMJD1A protein stability is controlled by the ubiquitin ligase STUB1. High levels of JMJD1A were strongly correlated with low STUB1 levels in human CRPC specimens. STUB1 inhibited AR activity, AR-V7 levels, and prostate cancer cell growth partly through degradation of JMJD1A. Furthermore, the acetyltransferase p300 acetylated JMJD1A at lysine (K) 421, a modification that recruits the BET family member BRD4 to block JMJD1A degradation and promote JMJD1A recruitment to AR targets. Increased levels of both total and K421-acetylated JMJD1A were observed in prostate cancer cells as they developed resistance to the AR antagonist enzalutamide. Treatment of prostate cancer cells with either p300 or BET inhibitors destabilized JMJD1A, and enzalutamide-resistant prostate cancer cells were more sensitive than parental cells to these inhibitors. Together, our findings identify a critical role for acetylation of JMJD1A in regulating JMJD1A stability and AR activity in CRPC. These newly identified mechanisms controlling JMJD1A protein stability provide potential druggable targets to encourage the development of additional therapies for advanced prostate cancer. Significance: Identification of mechanisms regulating JMJD1A protein stability reveals new strategies to destabilize JMJD1A and concomitantly inhibit AR activities as potential prostate cancer therapy.
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Overexpression of JMJD1A confers enzalutamide resistance to enzalutamide-sensitive prostate cancer cell lines.
“This mechanism is connected to drug resistance in prostate cancer cell lines as JMJD1AK421Ac levels were increased in resistant lines, partial knockdown of JMJD1A in resistant lines resensitized the cells to treatment, and overexpression of JMJD1A conferred enzalutamide resistance to enzalutamide-sensitive lines [112].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [112]
JMJD1A K421Ac levels are increased in enzalutamide-resistant prostate cancer cell lines.
“This mechanism is connected to drug resistance in prostate cancer cell lines as JMJD1AK421Ac levels were increased in resistant lines, partial knockdown of JMJD1A in resistant lines resensitized the cells to treatment, and overexpression of JMJD1A conferred enzalutamide resistance to enzalutamide-sensitive lines [112].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [112]
Acetylation of JMJD1A at K421 is a route for increasing androgen receptor activity and prostate cancer cell proliferation.
“Acetylation at K421 on histone demethylase JMJD1A is one such route for increasing AR activity and increasing prostate cancer cell proliferation [112].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [112]
p300-mediated acetylation of JMJD1A at K421 promotes its interaction with BRD4, disrupting binding of E3 ligase STUB1.
“However, when p300 acetylates JMJD1A at K421, it promotes JMJD1A’s interaction with BRD4 (an acetyllysine reader protein) which disrupts the ability of E3 ligase STUB1 to bind (Figure 6A).”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [112]
The BRD4-JMJD1A K421Ac interaction recruits JMJD1A to AR target genes and upregulates their transcription.
“The BRD4-JMJD1AK421Ac interaction therein recruits JMJD1A to AR target genes to upregulate their transcription (Figure 6A) [112].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [112]
Partial knockdown of JMJD1A in resistant prostate cancer cell lines resensitizes them to treatment.
“This mechanism is connected to drug resistance in prostate cancer cell lines as JMJD1AK421Ac levels were increased in resistant lines, partial knockdown of JMJD1A in resistant lines resensitized the cells to treatment, and overexpression of JMJD1A conferred enzalutamide resistance to enzalutamide-sensitive lines [112].”
From Acetylation: a new target for protein degradation in cancer (2025) · cites this paper as [112]
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- Authors
- Xu, S., Fan, L., Jeon, H.-Y., Zhang, F., Cui, X., Mickle, M. B., Peng, G., Hussain, A., Fazli, L., Gleave, M. E., Dong, X., & Qi, J.
- Affiliations
- University of Maryland, Baltimore (US)
- Baltimore VA Medical Center (US)
- University of British Columbia (CA)
- Corresponding author
- Qi, Jianfei
- ORCID
- Venue
- Cancer Research
- Published
- 2020-08-01
- Volume
- 80
- Issue
- 15
- Pages
- 3074-3087
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- PMC
- PMC7415556
- OpenAlex
- W3033104501
- Cited by
- 64
- References
- 49
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 13 · 2023: 16 · 2022: 10 · 2021: 6 · 2020: 2
- FWCI
- 4.79
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NCI (R01CA207118)
- Merit Review (I01 BX000545)
- Topics
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Prostate Cancer Treatment and Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- JMJD1A, P300, histone acetylation, STUB1, ubiquitin ligase, protein stability, androgen receptor, castration-resistant prostate cancer, AR-V7, BRD4, BET inhibitors, enzalutamide resistance
- MeSH terms
- PC-3 Cells, Bromodomain Containing Proteins, p300-CBP-Associated Factor, Acetylation, Animals, Cells, Cultured, Enzyme Activation, Humans, Male, Mice, Nude, Protein Processing, Post-Translational, Receptors, Androgen, Transcription Factors, Cell Cycle Proteins, Ubiquitin-Protein Ligases, p300-CBP Transcription Factors, Mice, Jumonji Domain-Containing Histone Demethylases, HEK293 Cells, Proteolysis, Prostatic Neoplasms, Castration-Resistant
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