Functional TRIM24 degrader via conjugation of ineffectual bromodomain and VHL ligands
Open accessAbstract
The addressable pocket of a protein is often not functionally relevant in disease. This is true for the multidomain, bromodomain-containing transcriptional regulator TRIM24. TRIM24 has been posited as a dependency in numerous cancers, yet potent and selective ligands for the TRIM24 bromodomain do not exert effective anti-proliferative responses. We therefore repositioned these probes as targeting features for heterobifunctional protein degraders. Recruitment of the VHL E3 ubiquitin ligase by dTRIM24 elicits potent and selective degradation of TRIM24. Using dTRIM24 to probe TRIM24 function, we characterize the dynamic genome-wide consequences of TRIM24 loss on chromatin localization and gene control. Further, we identify TRIM24 as a novel dependency in acute leukemia. Pairwise study of TRIM24 degradation versus bromodomain inhibition reveals enhanced anti-proliferative response from degradation. We offer dTRIM24 as a chemical probe of an emerging cancer dependency, and establish a path forward for numerous selective yet ineffectual ligands for proteins of therapeutic interest.
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When ineffectual bromodomain ligands were furnished into PROTAC targeting warheads, potent and selective degradation could be achieved.
“When ineffectual bromodomain ligands were furnished into PROTAC targeting warheads, potent and selective degradation could be achieved.45−47”
From Advancing Targeted Protein Degradation via Multiomics Profiling and Artificial Intelligence (2023) · cites this paper as [45]
Targeted protein degraders, also known as PROTACs, are an emerging strategy for ablating previously undruggable protein functions.
“Targeted protein degraders, also known as PROTACs (PROteolysis TArgeting Chimeras), are an emerging strategy for ablating previously undruggable protein functions”
From Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models (2019) · cites this paper as Gechijian et al., 2018
Targeted protein degradation approaches have expanded the landscape of druggable proteins by providing a mechanism to transform a non-functional protein binder into an effective targeted degrader.
“Targeted protein degradation approaches have expanded the landscape of druggable proteins by providing a mechanism to transform a non-functional protein binder into an effective targeted degrader”
From Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models (2019) · cites this paper as Gechijian et al., 2018
PROTACs targeting TRIM24, RIPK2, and JAK family enzymes may have potential to treat certain types of hematologic malignancies but require further studies.
“In addition, PROTACs targeting tripartite motif-containing protein 24 (TRIM24), receptor-interacting protein kinase 2 (RIPK2), and the Janus kinase family enzymes for degradation may also have the potential to be used to treat certain types of hematologic malignancies but require further studies [185–187].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [185]
Protein domains that feature ligandable binding pockets but are not involved in the pathogenic function of a gene can be favourably targeted by PROTACs.
“Protein domains that feature ligandable binding pockets but are not involved in the pathogenic function of a gene can be favourably targeted by these molecules 26,27 ,”
From Targeted protein degradation: expanding the toolbox (2019) · cites this paper as [27]
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Self-citation
- Authors
- Gechijian, L. N., Buckley, D. L., Lawlor, M. A., Reyes, J. M., Paulk, J., Ott, C. J., Winter, G. E., Erb, M. A., Scott, T. G., Xu, M., Seo, H.-S., Dhe-Paganon, S., Kwiatkowski, N. P., Perry, J. A., Qi, J., Gray, N. S., & Bradner, J. E.
- Affiliations
- Dana-Farber Cancer Institute (US)
- Harvard University (US)
- Corresponding author
- Gray, Nathanael S.
- Bradner, James E.
- ORCID
- Venue
- Nature Chemical Biology
- Published
- 2018-03-05
- Volume
- 14
- Issue
- 4
- Pages
- 405-412
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC5866761
- OpenAlex
- W2792397649
- Cited by
- 222
- References
- 54
- Citations by year
- 2026: 15 · 2025: 19 · 2024: 15 · 2023: 21 · 2022: 29 · 2021: 40 · 2020: 35 · 2019: 35 · 2018: 13
- FWCI
- 11.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Novartis
- National Cancer Institute (P50CA206963, P01CA066996)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- TRIM24, bromodomain, VHL E3 ubiquitin ligase, protein degradation, bromodomain inhibitors, acute leukemia, cancer dependency, chemical probes, chromatin localization, gene expression regulation, drug repurposing
- MeSH terms
- Protein Domains, Animals, Carrier Proteins, Humans, Ligands, Nuclear Proteins, Protein Binding, Transcription Factors, Leukemia, Myeloid, Acute, Gene Expression Regulation, Neoplastic, Mutagenesis, 3T3 Cells, Crystallography, X-Ray, RNA, Small Interfering, Cell Line, Tumor, Proteasome Endopeptidase Complex, Cell Proliferation, Mice, HEK293 Cells, MCF-7 Cells
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