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Stabilization of the Max Homodimer with a Small Molecule Attenuates Myc-Driven Transcription
Open accessAbstract
The transcription factor Max is a basic-helix-loop-helix leucine zipper (bHLHLZ) protein that forms homodimers or interacts with other bHLHLZ proteins, including Myc and Mxd proteins. Among this dynamic network of interactions, the Myc/Max heterodimer has crucial roles in regulating normal cellular processes, but its transcriptional activity is deregulated in a majority of human cancers. Despite this significance, the arsenal of high-quality chemical probes to interrogate these proteins remains limited. We used small molecule microarrays to identify compounds that bind Max in a mechanistically unbiased manner. We discovered the asymmetric polycyclic lactam, KI-MS2-008, which stabilizes the Max homodimer while reducing Myc protein and Myc-regulated transcript levels. KI-MS2-008 also decreases viable cancer cell growth in a Myc-dependent manner and suppresses tumor growth in vivo. This approach demonstrates the feasibility of modulating Max with small molecules and supports altering Max dimerization as an alternative approach to targeting Myc.
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“In 2019, Struntz et al. utilized SMM (small molecule microarray) screening to identify KI-MS2-001 (168) (IC50 = 1.98 μM), a molecule with a unique asymmetric polycyclic lactam compound.422”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
In the citing paper
“Experimental data indicate that KI-MS2-008 is effective in reducing tumor size at a low dose (0.06 mg·kg−1, iv) in mouse T-cell acute lymphoblastic leukemia (T-ALL) transplant tumor models.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
In the citing paper
“Thus, stabilizing the Max-Max homodimer can prevent Myc-Max transactivation of target genes.422”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
In the citing paper
“On the other hand, formation of Max-Max homodimer provides an alternative mechanism for blocking Myc/Max interactions and preventing Myc/Max heterodimers from binding to DNA, resulting in reduced transcriptional activity.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
In the citing paper
“Further structural optimization led to the development of KI-MS2-008 (IC50 = 1.28 μM), which exhibits significantly increased binding affinity for Max-Max homodimers, reduces Myc protein levels, perturbs Myc-driven transcriptional programs, induces Myc-dependent cellular differentiation, and affects viable cell growth of both engineered and non-engineered cell lines.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [422]
In the citing paper
“KI-MS2-008 (Fig. 6), an optimized analog of one of the drug hits, stabilizes Max homodimers and thus renders Max less capable of binding Myc.107”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [107]
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Metadata
- Authors
- Struntz, N. B., Chen, A., Deutzmann, A., Wilson, R. M., Stefan, E., Evans, H. L., Ramirez, M. A., Liang, T., Caballero, F., Wildschut, M. H. E., Neel, D. V., Freeman, D. B., Pop, M. S., McConkey, M., Muller, S., Curtin, B. H., Tseng, H., Frombach, K. R., Butty, V. L., Levine, S. S., Feau, C., Elmiligy, S., Hong, J. A., Lewis, T. A., Vetere, A., Clemons, P. A., Malstrom, S. E., Ebert, B. L., Lin, C. Y., Felsher, D. W., & Koehler, A. N.
- Affiliations
- Koch Institute for Integrative Cancer Research At MIT (US)
- Stanford Medicine (US)
- Baylor College of Medicine (US)
- Cambridge Intellectual Property (United Kingdom) (GB)
- Broad Institute (US)
- Boston Children's Hospital (US)
- Corresponding author
- Koehler, Angela N.
- ORCID
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2019-05
- Volume
- 26
- Issue
- 5
- Pages
- 711-723.e14
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- OpenAlex
- W2921930449
- Cited by
- 130
- References
- 76
- Citations by year
- 2026: 9 · 2025: 24 · 2024: 22 · 2023: 11 · 2022: 8 · 2021: 25 · 2020: 20 · 2019: 11
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell chemical biology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- DSpace@MIT (Massachusetts Institute of Technology) (submittedVersion, cc-by-nc-nd)
- Funders
- National Cancer Institute (R01-CA160860, P30-CA14051)
- Koch Institute Cancer Center (U01-CA176152)
- NIH (CA170378PQ2, 1U01CA188383-01/S1, 1R01CA215452-01)
- Leukemia & Lymphoma Society
- Ono Pharma Foundation
- MIT Deshpande Center
- MIT Center for Precision Cancer Medicine
- AACR
- Merkin Institute
- Cancer Prevention Research Institute of Texas (RR150093)
- MIT
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- Max protein, Myc-Max heterodimer, bHLH transcription factors, small molecule inhibitors, tumor cell growth inhibition, tumor growth inhibition, chemical probes
- MeSH terms
- Animals, Cell Line, Disease Models, Animal, Humans, Lactams, Male, Neoplasms, Polycyclic Compounds, Promoter Regions, Genetic, Protein Binding, Repressor Proteins, Transcription, Genetic, Ultraviolet Rays, Proto-Oncogene Proteins c-myc, Mice, SCID, Mice, Inbred NOD, Dimerization, Mice, Rats, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Small Molecule Libraries
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