Bromodomain Protein BRD4 Is a Transcriptional Repressor of Autophagy and Lysosomal Function
Open accessAbstract
Autophagy is a membrane-trafficking process that directs degradation of cytoplasmic material in lysosomes. The process promotes cellular fidelity, and while the core machinery of autophagy is known, the mechanisms that promote and sustain autophagy are less well defined. Here we report that the epigenetic reader BRD4 and the methyltransferase G9a repress a TFEB/TFE3/MITF-independent transcriptional program that promotes autophagy and lysosome biogenesis. We show that BRD4 knockdown induces autophagy in vitro and in vivo in response to some, but not all, situations. In the case of starvation, a signaling cascade involving AMPK and histone deacetylase SIRT1 displaces chromatin-bound BRD4, instigating autophagy gene activation and cell survival. Importantly, this program is directed independently and also reciprocally to the growth-promoting properties of BRD4 and is potently repressed by BRD4-NUT, a driver of NUT midline carcinoma. These findings therefore identify a distinct and selective mechanism of autophagy regulation.
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BRD4 inhibition induces autophagic gene expression.
“BRD4 inhibition has recently been reported to induce autophagic gene expression22.”
From A BET family protein degrader provokes senolysis by targeting NHEJ and autophagy in senescent cells (2020) · cites this paper as [22]
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- Authors
- Sakamaki, J.-I., Wilkinson, S., Hahn, M., Tasdemir, N., O’Prey, J., Clark, W., Hedley, A., Nixon, C., Long, J. S., New, M., Van Acker, T., Tooze, S. A., Lowe, S. W., Dikic, I., & Ryan, K. M.
- Affiliations
- Cancer Research UK Scotland Institute (GB)
- Goethe University Frankfurt (DE)
- Memorial Sloan Kettering Cancer Center (US)
- The Francis Crick Institute (GB)
- Corresponding author
- Ryan, Kevin M.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2017-05
- Volume
- 66
- Issue
- 4
- Pages
- 517-532.e9
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC5446411
- OpenAlex
- W2614434863
- Cited by
- 249
- References
- 64
- Citations by year
- 2026: 21 · 2025: 21 · 2024: 22 · 2023: 29 · 2022: 32 · 2021: 41 · 2020: 34 · 2019: 22 · 2018: 22 · 2017: 5
- FWCI
- 18.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (acceptedVersion)
- Figshare (submittedVersion, cc-by)
- Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) (submittedVersion, cc-by)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, cc-by)
- Funders
- Cancer Research UK
- Astellas Pharma
- Worldwide Cancer Research
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
- Keywords
- BRD4, autophagy, lysosomal biogenesis, transcriptional repression, epigenetic reader protein, G9a, histone methyltransferase, starvation, AMPK, SIRT1, histone deacetylase, NUT midline carcinoma, chromatin binding, cell survival
- MeSH terms
- Bromodomain Containing Proteins, Animals, Autophagy, Chromatin, Drosophila melanogaster, Energy Metabolism, Histocompatibility Antigens, Humans, Lysosomes, Mice, Inbred C57BL, Mice, Transgenic, Nuclear Proteins, Pancreatic Neoplasms, Protein Binding, Histone-Lysine N-Methyltransferase, Time Factors, Transcription Factors, Transcription, Genetic, Transfection, Signal Transduction, Oncogene Proteins, Fusion, Down-Regulation, Gene Expression Regulation, Neoplastic, Cell Cycle Proteins, Carcinoma, Pancreatic Ductal, Drosophila Proteins, RNA Interference, Cell Line, Tumor, Cell Proliferation, AMP-Activated Protein Kinases, Sirtuin 1, HEK293 Cells, TOR Serine-Threonine Kinases, Proteolysis, Protein Aggregates
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