BET Bromodomain Proteins Function as Master Transcription Elongation Factors Independent of CDK9 Recruitment
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Processive elongation of RNA Polymerase II from a proximal promoter paused state is a rate-limiting event in human gene control. A small number of regulatory factors influence transcription elongation on a global scale. Prior research using small-molecule BET bromodomain inhibitors, such as JQ1, linked BRD4 to context-specific elongation at a limited number of genes associated with massive enhancer regions. Here, the mechanistic characterization of an optimized chemical degrader of BET bromodomain proteins, dBET6, led to the unexpected identification of BET proteins as master regulators of global transcription elongation. In contrast to the selective effect of bromodomain inhibition on transcription, BET degradation prompts a collapse of global elongation that phenocopies CDK9 inhibition. Notably, BRD4 loss does not directly affect CDK9 localization. These studies, performed in translational models of T cell leukemia, establish a mechanism-based rationale for the development of BET bromodomain degradation as cancer therapy.
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dBET6 and ARV-771 have matched cellular potency, including in KBM7 cells.
“we focused on two BET Bromodomain targeting PROTACs: dBET6 (CRBN-based) and ARV-771 (VHL-based) that have matched cellular potency, including in the near-haploid human leukemia cell line KBM7 (Extended Data Fig. 1A)26,27.”
From Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders (2023) · cites this paper as [27]
Differences in proteome response could be attributed to distinct recruitment ligases used by MZ1 (VHL) or dBET6 (CRBN), as well as established differences in selectivity for BBDs, where MZ1 preferentially degrades BRD4, whereas dBET6 degrades BRD2, BRD3 and BRD4 equivalently.
“These differences could be attributed to the distinct recruitment ligases used by MZ1 (VHL) or dBET6 (CRBN), as well as the established differences in selectivity for the BBDs, where MZ1 preferentially degrades BRD4 (17), whereas dBET6 degrades BRD2, BRD3 and BRD4, equivalently (16).”
From The drug efflux pump MDR1 promotes intrinsic and acquired resistance to PROTACs in cancer cells (2022) · cites this paper as [16]
dBET6 showed better efficacy against T-ALL compared with JQ1.
“Later, they optimized the linker and found a more potent PROTAC (dBET6) that showed better efficacy against T-ALL compared with JQ1 [43].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [43]
Profiling changes in global protein expression by proteomics will be helpful to appreciate potential off-target toxicities of PROTACs.
“Therefore, profiling the changes in global protein expression by proteomics will be helpful to appreciate the potential off-target toxicities of PROTACs [3, 4, 43].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [43]
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- Authors
- Winter, G. E., Mayer, A., Buckley, D. L., Erb, M. A., Roderick, J. E., Vittori, S., Reyes, J. M., di Iulio, J., Souza, A., Ott, C. J., Roberts, J. M., Zeid, R., Scott, T. G., Paulk, J., Lachance, K., Olson, C. M., Dastjerdi, S., Bauer, S., Lin, C. Y., Gray, N. S., Kelliher, M. A., Churchman, L. S., & Bradner, J. E.
- Affiliations
- Austrian Academy of Sciences (AT)
- Harvard University (US)
- Dana-Farber Cancer Institute (US)
- University of Massachusetts Chan Medical School (US)
- Corresponding author
- Churchman, L. Stirling
- Bradner, James E.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2017-07
- Volume
- 67
- Issue
- 1
- Pages
- 5-18.e19
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC5663500
- OpenAlex
- W2733066269
- Cited by
- 465
- References
- 47
- Citations by year
- 2026: 43 · 2025: 59 · 2024: 44 · 2023: 54 · 2022: 66 · 2021: 59 · 2020: 43 · 2019: 50 · 2018: 42 · 2017: 5
- FWCI
- 15.64
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- The Journal of the American Medical Association (JAMA) Network (American Medical Association) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
- Funders
- William Lawrence and Blanche Hughes Foundation
- NIH (R01-HG007173, R01-GM117333, R01-CA176745, P01-CA109901)
- EMBO long-term fellowship (ALTF 39-2013)
- Damon Runyon Cancer Research Foundation (DRG-2196-14)
- Human Frontier Science Program (LT000314/2013-L)
- EMBO (ALTF858-2012)
- Swiss National Science Foundation Postdoc Mobility Fellowship
- American Cancer Society Post-doctoral fellowship (125087-PF-13-247-01-LIB)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- BET proteins, BRD4, transcription elongation, RNA polymerase II, CDK9, bromodomain inhibitors, JQ1, enhancers, T-cell leukemia, cancer therapy
- MeSH terms
- Bromodomain Containing Proteins, Animals, Antineoplastic Agents, DNA-Binding Proteins, Dose-Response Relationship, Drug, Female, Humans, Mice, Transgenic, Nuclear Proteins, Peptide Hydrolases, RNA Polymerase II, Time Factors, Transcription Factors, Transfection, Gene Expression Regulation, Leukemic, Mice, SCID, Mice, Inbred NOD, Cell Cycle Proteins, Jurkat Cells, Xenograft Model Antitumor Assays, Cyclin-Dependent Kinase 9, Ubiquitin-Protein Ligases, HCT116 Cells, Multiprotein Complexes, Adaptor Proteins, Signal Transducing, Precursor T-Cell Lymphoblastic Leukemia-Lymphoma, Protein Stability, HEK293 Cells, Proteolysis, Transcription Elongation, Genetic
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