Formation of a structurally-stable conformation by the intrinsically disordered MYC:TRRAP complex
Open accessAbstract
Our primary goal is to therapeutically target the oncogenic transcription factor MYC to stop tumor growth and cancer progression. Here, we report aspects of the biophysical states of the MYC protein and its interaction with one of the best-characterized MYC cofactors, TRansactivation/tRansformation-domain Associated Protein (TRRAP). The MYC:TRRAP interaction is critical for MYC function in promoting cancer. The interaction between MYC and TRRAP occurs at a precise region in the MYC protein, called MYC Homology Box 2 (MB2), which is central to the MYC transactivation domain (TAD). Although the MYC TAD is inherently disordered, this report suggests that MB2 may acquire a defined structure when complexed with TRRAP which could be exploited for the investigation of inhibitors of MYC function by preventing this protein-protein interaction (PPI). The MYC TAD, and in particular the MB2 motif, is unique and invariant in evolution, suggesting that MB2 is an ideal site for inhibiting MYC function.
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TRRAP is a key cofactor of Myc and a member of the histone acetylation (HAT) complex that assists TFs such as Myc in controlling gene expression.
“It is a key cofactor of Myc and a member of the histone acetylation (HAT) complex that assists TFs such as Myc in controlling gene expression.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [430]
Transformation/transcription domain associated protein (TRRAP) is a highly conservative 434 kDa protein that belongs to the phosphatidylinositol 3-kinase related kinase (PI3K) family.
“Transformation/transcription domain associated protein (TRRAP) is a highly conservative 434 kDa protein that belongs to the phosphatidylinositol 3-kinase related kinase (PI3K) family.430”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [430]
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Undruggable oncoproteins cMyc and NMyc bind to mediator of transcription with superior high affinityPreprint
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Llombart, V., O’Connor, D., Demeulemeester, J., Bhamra, A., Šurinová, S., Turňa, A., Fung, K. T. M., Wang, L., Li, Y., Rapoz-D’Silva, T., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.16.659507
Kars, G., Becker, P. B., & Apostolou, Z. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag178
Henchy, C., Wang, H., & Prochownik, E. V. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.22.733817
BindingDB Entry 50018504: Targeting MYC: From understanding its biology to drug discovery.
BindingDB (2024) · UC San Diego · doi:10.7270/q2qz2g61
- Authors
- Feris, E. J., Hinds, J. W., & Cole, M. D.
- Affiliations
- Dartmouth College (US)
- Corresponding author
- Cole, Michael D.
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2019-12-02
- Volume
- 14
- Issue
- 12
- Pages
- e0225784
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC6886782
- OpenAlex
- W2991244815
- Cited by
- 29
- References
- 64
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 9 · 2020: 2
- FWCI
- 1.24
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- National Cancer Institute (5R01CA055248-25)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- c-Myc, TRRAP, intrinsically disordered proteins, protein-protein interaction, protein complex structure, oncogenic transcription factor, MYC inhibitors, cancer therapy
- MeSH terms
- Humans, Nuclear Proteins, Protein Binding, Protein Conformation, Proto-Oncogene Proteins c-myc, Ethylene Glycol, Adaptor Proteins, Signal Transducing, Protein Stability, HEK293 Cells, Intrinsically Disordered Proteins, Proton Magnetic Resonance Spectroscopy
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