Polymerization of ZBTB transcription factors regulates chromatin occupancy
Open accessAbstract
BCL6, an oncogenic transcription factor (TF), forms polymers in the presence of a small-molecule molecular glue that stabilizes a complementary interface between homodimers of BCL6's broad-complex, tramtrack, and bric-à-brac (BTB) domain. The BTB domains of other proteins, including a large class of TFs, have similar architectures and symmetries, raising the possibility that additional BTB proteins self-assemble into higher-order structures. Here, we surveyed 189 human BTB proteins with a cellular fluorescent reporter assay and identified 18 ZBTB TFs that show evidence of polymerization. Through biochemical and cryoelectron microscopy (cryo-EM) studies, we demonstrate that these ZBTB TFs polymerize into filaments. We found that BTB-domain-mediated polymerization of ZBTB TFs enhances chromatin occupancy within regions containing homotypic clusters of TF binding sites, leading to repression of target genes. Our results reveal a role of higher-order structures in regulating ZBTB TFs and suggest an underappreciated role for TF polymerization in modulating gene expression.
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Few studies have conclusively shown that TF multimerisation is a pre-requisite for efficient DNA-binding, but more recent works on BTB domain proteins and FOXP3 have suggested that higher-order assemblies of these TFs are needed for their cellular functions.
“Few studies have conclusively shown that TF multimerisation is a pre-requisite for efficient DNA-binding (e.g. SOX6 73 ), but more recent works on BTB domain proteins 74 and FOXP3 75 have suggested that higher-order assemblies of these TFs are needed for their cellular functions.”
From Tetramerisation governs SALL transcription factor function in development and disease (2025) · cites this paper as [74]
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Schulten, A., Jang, G., Payne-Dwyer, A. L., Fiedler, M., Nielsen, M., Mateo‐Bonmatí, E., Bienz, M., Leake, M. C., & Dean, C. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.002 · Cited by 11 · see citing works
Horton, J. R., Yu, M., Zhou, J., Tran, M. L., Anakal, R. R., Lu, Y., Blumenthal, R., Zhang, X., Huang, Y., Zhang, X., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58998-7 · Cited by 11 · see citing works
“I have a number of questions and comments for the authors For the structure of ZF4-6 bound to a 20mer from the globin locus, are you confident that modules B and C really bind or are these artefacts in the crystal structure.”
Brovkina, M. V., & Clowney, E. J. (2026) · bioRxiv · doi:10.64898/2026.04.14.718444 · Cited by 1 · see citing works
“Vertebrate BTB-ZFs have been thought to prefer dimer configurations, but recent work has shown that they too can polymerize – polymerization increases DNA binding and repressive activity at loci with clusters of homotypic motifs in a dose-dependent manner (Mance et al., 2024; Park et al., 2024).”
Molecular Glue Degraders Redefining Targeted Therapies From Discovery to Therapeutic Applications
Wen, J., Yu, J., Wen, W., & Jiang, B. (2026) · MedComm – Oncology · doi:10.1002/mog2.70058
Structure–Function Correlations in KCTD1/KCTD15 Proteins
Balasco, N., & Vitagliano, L. (2025) · The 5th International Symposium on Frontiers in Molecular Science · doi:10.3390/blsf2025053002 · Cited by 1 · see citing works
“Indeed, it has been demonstrated that BTB domains, through self-interaction, can exhibit a wide range of oligomeric states, ranging from monomers to polymers [16].”
Decoding the role of zinc finger proteins in urological malignancies
Yang, L. X., Gan, Y., Fan, Y., & Zhang, Q. (2025) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2025.189470 · Cited by 1 · see citing works
Structural insights into ZBTB20 action at the AFP promoter.
Yang, L., Xie, H., Wan, X., Li, M., Lv, M.-Q., Duan, Y., Shi, Y.-Y., Zhang, W.-P. J., & Li, F.-D. (2025) · Structure · doi:10.1016/j.str.2025.05.009 · Cited by 1 · see citing works
Tetramerisation governs SALL transcription factor function in development and disease
Giuliani, S., Chhatbar, K., Wear, M., Guy, J., Mathieson, T., Burdett, H., George, L., Alston, G., Spanos, C., McHugh, T., et al. (2025) · bioRxiv · doi:10.1101/2025.10.27.684836
Zhang, Z.-H., Li, M., Feng, J.-L., Li, J.-A., & Zhang, L. (2026) · Clinical and Translational Medicine · doi:10.1002/ctm2.70848
“While ZBTB family members are traditionally considered transcriptional regulators, 36–38 our work reveals ZBTB10 as a functional orchestrator of K63 linkage assembly and autophagy initiation, expanding its biological scope into metabolic governance in cancer.”
ZBTB Transcription Factors Refine Cohesin Recruitment at Gene Promoters beyond CTCF
Bakim, S., MUTLU, E. G., Hakanoglu, N., & Uyar, E. (2026) · Cytology and Genetics · doi:10.3103/s0095452726050038
“Notably, the recent discovery that ZBTB transcription factors polymerize into filaments through their BTB domains (Park et al., 2024) suggests a plausible mechanism by which ZBTB7B and ZBTB21 could stabilize cohesin at promoters through cooperative, multivalent chromatin binding.”
A new class of inherently efficient SUMOylation substrates
Cisse, E. H., Visticot, L., Cepa, R., Mishra, A., Coste, F., Goffinont, S., Mance, L., Battault, S., Guigneau, D., Talhaoui, I., et al. (2026) · bioRxiv · doi:10.64898/2026.09.10.750468
“Recently, our group and another team have independently characterised a subset of ZBTB proteins – estimated to include around twenty distinct proteins (40% of the ZBTB family) in humans – whose BTB domains form filamentous structures composed of dimers 71,73 .”
Developmental trajectory and regulation of primary males in giant grouper (Epinephelus lanceolatus)
Jiang, G., Zhao, Z., Zheng, X., Wu, Z.-Y., Zhang, R., Nie, J.-Y., Chen, Z.-F., Wang, X.-S., Du, H., Ye, D., et al. (2026) · Water Biology and Security · doi:10.1016/j.watbs.2026.100706
Kim, T.-Y., Park, J.-H., Jung, Y. W., Lee, J., & Kim, J. (2026) · Medicina · doi:10.3390/medicina62071244
“ZBTB factors recruit coactivators or robust corepressor complexes via these PPIs, including N-CoR, SMRT, and histone deacetylases (HDACs), to specific chromatin loci, thereby orchestrating extensive chromatin remodeling and transcriptional regulation [55,56].”
Self-citationTranscriptional control of brain sex differentiation in Diptera
Brovkina, M. V., & Clowney, E. J. (2026) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2026.103199
Opposing Roles of CREPT and p15RS in Tumorigenesis via Differential Regulation of Wnt Signaling
Zhou, D., Li, J., Ren, F., Cao, Y., Ning, B., Wang, W.-C., Jia, B.-Q., Li, G.-M., Wang, Y.-Y., & Chang, Z.-J. (2026) · Cancers · doi:10.3390/cancers18121911
“Accumulating evidence has demonstrated that protein oligomerization is crucial for the regulation of multiple cellular processes [45,50], as well as for the function of CREPT [32].”
A ZBTB26–Integrator Axis Mediates Targeted Transcriptional Activation
Yu, D., Chen, G.-Y., Lin, F., Cheng, X., Qiao, Z.-J., Zhu, P., & Hu, S. (2026) · The FASEB Journal · doi:10.1096/fj.202504190r
“These factors primarily function as transcriptional repressors through BTB domain-mediated protein interactions, including recruitment of corepressors and organization of higher-order homomeric assemblies [4, 5].”
Nucleosomes constrain 1D DNA diffusion by eukaryotic transcription factors
(2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01658-7
- Authors
- Park, P. M. C., Park, J., Brown, J., Hunkeler, M., Roy Burman, S. S., Donovan, K. A., Yoon, H., Nowak, R. P., Słabicki, M., Ebert, B. L., & Fischer, E. S.
- Affiliations
- Broad Institute (US)
- Harvard University (US)
- Corresponding author
- Ebert, Benjamin L.
- Fischer, Eric S.
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2024-07
- Volume
- 84
- Issue
- 13
- Pages
- 2511-2524.e8
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC11305084
- OpenAlex
- W4400537798
- Cited by
- 22
- References
- 69
- Citations by year
- 2026: 8 · 2025: 11 · 2024: 3
- FWCI
- 2.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 375 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- Funders
- National Institutes of Health (R35CA253125, R01HL082945, P01CA066996, P50CA206963)
- Howard Hughes Medical Institute
- Astellas Pharma US
- Edward P. Evans Foundation
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- Harvard Medical School
- AbbVie
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- BTB domain, protein polymerization, chromatin occupancy, transcriptional repression, BCL6, molecular glues, protein filament assembly, protein higher-order structure, gene expression regulation
- MeSH terms
- Binding Sites, Chromatin, Gene Expression Regulation, Humans, Protein Binding, Transcription Factors, Cryoelectron Microscopy, Protein Multimerization, HEK293 Cells, Polymerization
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