The Diarylheptanoid Curcumin Induces MYC Inhibition and Cross-Links This Oncoprotein to the Coactivator TRRAP
Open accessAbstract
The c-Myc protein (MYC) is a transcription factor with strong oncogenic potential controlling fundamental cellular processes. In most human tumors, MYC is overexpressed by enhanced transcriptional activation, gene amplification, chromosomal rearrangements, or increased protein stabilization. To pharmacologically suppress oncogenic MYC functions, multiple approaches have been applied either to inhibit transcriptional activation of the endogenous MYC gene, or to interfere with biochemical functions of aberrantly activated MYC. Other critical points of attack are targeted protein modification, or destabilization leading to a non-functional MYC oncoprotein. It has been claimed that the natural compound curcumin representing the principal curcumoid of turmeric (Curcuma longa) has anticancer properties although its specificity, efficacy, and the underlying molecular mechanisms have been controversially discussed. Here, we have tested curcumin’s effect on MYC-dependent cell transformation and transcriptional activation, and found that this natural compound interferes with both of these MYC activities. Furthermore, in curcumin-treated cells, the endogenous 60-kDa MYC protein is covalently and specifically cross-linked to one of its transcriptional interaction partners, namely the 434-kDa transformation/transcription domain associated protein (TRRAP). Thereby, endogenous MYC levels are strongly reduced and cells stop to proliferate. TRRAP is a multidomain adaptor protein of the phosphoinositide 3-kinase-related kinases (PIKK) family and represents an important component of many histone acetyltransferase (HAT) complexes. TRRAP is important to mediate transcriptional activation executed by the MYC oncoprotein, but on the other hand TRRAP also negatively regulates protein stability of the tumor suppressor p53 (TP53). Curcumin-mediated covalent binding of MYC to TRRAP reduces the protein amounts of both interaction partners but does not downregulate TP53, so that the growth-arresting effect of wild type TP53 could prevail. Our results elucidate a molecular mechanism of curcumin action that specifically and irreversibly targets two crucial multifunctional cellular players. With regard to their broad impact in cancer, our findings contribute to explain the pleiotropic functions of curcumin, and suggest that this natural spice, or more bioavailable derivatives thereof, may constitute useful adjuvants in the therapy of MYC-dependent and TRRAP-associated human tumors.
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In 2021, Alexander et al. discovered curcumin interferes with the fundamental function of Myc and induces cross-linking between this oncogenic TF and its co-activator, TRRAP.
“In 2021, Alexander et al. discovered curcumin interferes with the fundamental function of Myc and induces cross-linking between this oncogenic TF and its co-activator, TRRAP.431”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [431]
The interaction between Myc and TRRAP takes place in a precise region of the Myc protein called MB-II, which is also at the core of the Myc transactivation domain (TAD).
“The interaction between Myc and TRRAP takes place in a precise region of the Myc protein called MB-II, which is also at the core of the Myc transactivation domain (TAD).431”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [431]
Covalent cross-linking of TRRAP with Myc can permanently isolate TRRAP, resulting in interference in the binding balance between TRRAP and its tumor suppressor partners.
“Covalent cross-linking of TRRAP with Myc can permanently isolate TRRAP, resulting in interference in the binding balance between TRRAP and its tumor suppressor partners.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [431]
Consequently, the endogenous Myc levels were drastically decreased, and cell proliferation was inhibited.
“Consequently, the endogenous Myc levels were drastically decreased, and cell proliferation was inhibited.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [431]
Experiments showed that in the presence of curcumin, endogenous Myc protein levels were significantly reduced, while constitutive expression of ectopic v-Myc was almost unaffected.
“Experiments showed that in the presence of curcumin, endogenous Myc protein levels were significantly reduced, while constitutive expression of ectopic v-Myc was almost unaffected.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [431]
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“However, cross-linking of the transient MYC/ TRRAP interaction by curcumin leads to a reduction of endogenous MYC protein levels and the cells stop to proliferate (93).”
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“…that curcumin promotes specific cross-linking of the master regulator MYC with its known protein partner TRRAP (transformation/transcription domain associated protein) without shortening the half-lives of the two proteins, thus reducing the proliferation of cancer cells (Mödlhammer et al. 2021).”
- Authors
- Mödlhammer, A., Pfurtscheller, S., Feichtner, A., Hartl, M., & Schneider, R.
- Affiliations
- Universität Innsbruck (AT)
- Corresponding author
- Hartl, Markus
- Venue
- Frontiers in Oncology
- Publisher
- Frontiers Media SA
- Published
- 2021-04-15
- Volume
- 11
- Pages
- 660481-660481
- ISSN
- 2234-943X (ISSN-L)
- PMC
- PMC8082493
- OpenAlex
- W3155380340
- Cited by
- 7
- References
- 68
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2021: 2
- FWCI
- 0.40
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Oncology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Digital Library of the University of Innsbruck (University of Innsbruck) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Austrian Science Fund (FWF-TRP-233-B18)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Curcumin's Biomedical Applications
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioactive natural compounds
- Keywords
- curcumin, c-Myc, TRRAP, protein-protein cross-linking, TP53, histone acetyltransferase complexes, anticancer natural compounds
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