The MYC transcription factor network: balancing metabolism, proliferation and oncogenesis

Modularity and community structure in networks

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Master Transcription Factors and Mediator Establish Super-Enhancers at Key Cell Identity Genes

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Cell-specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor

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The transcription factor Myc controls metabolic reprogramming upon T lymphocyte activation

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Max: A Helix-Loop-Helix Zipper Protein That Forms a Sequence-Specific DNA-Binding Complex with Myc

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Reflecting on 25 years with MYC

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A genomic regulatory network for development

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Transcriptional Amplification in Tumor Cells with Elevated c-Myc

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An Extended Transcriptional Network for Pluripotency of Embryonic Stem Cells

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c-Myc Regulates Transcriptional Pause Release

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c-Myc Is a Universal Amplifier of Expressed Genes in Lymphocytes and Embryonic Stem Cells

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The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation

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Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression

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Myc’s broad reach

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PCGF Homologs, CBX Proteins, and RYBP Define Functionally Distinct PRC1 Family Complexes

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MYC Activation Is a Hallmark of Cancer Initiation and MaintenancePreprint

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A Complex with Chromatin Modifiers That Occupies E2F- and Myc-Responsive Genes in G 0 Cells

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Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites

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Histone Deacetylase Activity Is Required for Full Transcriptional Repression by mSin3A

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Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain

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Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity

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Mad-max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3

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Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex

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Functional role for c-myc in mitogenic response to platelet-derived growth factor

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DNA-dependent formation of transcription factor pairs alters their binding specificity

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Cooperative Binding of Transcription Factors Orchestrates Reprogramming

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X-Ray Structures of Myc-Max and Mad-Max Recognizing DNA

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Exome sequencing identifies MAX mutations as a cause of hereditary pheochromocytoma

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MYC: Connecting selective transcriptional control to global RNA production

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Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells.

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MYC degradation

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Pan-cancer Alterations of the MYC Oncogene and Its Proximal Network across the Cancer Genome Atlas

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Three new types of viral oncogene of cellular origin specific for haematopoietic cell transformation

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An Overview of MYC and Its Interactome

Conacci-Sorrell, M., McFerrin, L., & Eisenman, R. N. (2014) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a014357 · Cited by 408 · see citing works

Correction to: The Brachyury gene encodes a novel DNA binding protein.

Kispert, A., & Hermann, B. G. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06179.x · Cited by 406 · see citing works

A genome-wide RNAi screen identifies a new transcriptional module required for self-renewalPreprint

Hu, G., Kim, J., Xu, Q., Leng, Y., Orkin, S. H., & Elledge, S. J. (2009) · Genes & Development · doi:10.1101/gad.1769609 · Cited by 393 · see citing works

Transcription Factor Binding in Human Cells Occurs in Dense Clusters Formed around Cohesin Anchor Sites

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Myc-binding-site recognition in the human genome is determined by chromatin context

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Mad3 and Mad4: novel Max‐interacting transcriptional repressors that suppress c‐myc dependent transformation and are expressed during neural and epidermal differentiation.

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Regulation of cyclin D2 gene expression by the Myc/Max/Mad network: Myc-dependent TRRAP recruitment and histone acetylation at the cyclin D2 promoterPreprint

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The Brachyury gene encodes a novel DNA binding protein.

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DNA-dependent formation of transcription factor pairs alters their binding specificity

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Interaction with WDR5 Promotes Target Gene Recognition and Tumorigenesis by MYC

Thomas, L. R., Wang, Q., Grieb, B. C., Phan, J., Foshage, A. M., Sun, Q., Olejniczak, E. T., Clark, T., Dey, S., Lorey, S., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.02.028 · Cited by 310 · see citing works

A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation.Preprint

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The T protein encoded by Brachyury is a tissue‐specific transcription factor.

Kispert, A., Koschorz, B., & Herrmann, B. G. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb00158.x · Cited by 292 · see citing works

Glucose sensing by MondoA:Mlx complexes: a role for hexokinases and direct regulation of thioredoxin-interacting protein expression

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Response of BRAF -Mutant Melanoma to BRAF Inhibition Is Mediated by a Network of Transcriptional Regulators of Glycolysis

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DNA and RNA from Uninfected Vertebrate Cells Contain Nucleotide Sequences Related to the Putative Transforming Gene of Avian Myelocytomatosis Virus

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MYC Disrupts the Circadian Clock and Metabolism in Cancer Cells

Altman, B. J., Hsieh, A. L., Sengupta, A., Krishnanaiah, S. Y., Stine, Z. E., Walton, Z. E., Gouw, A. M., Venkataraman, A., Li, B., Goraksha-Hicks, P., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.003 · Cited by 273 · see citing works

Two main genetic pathways lead to the transformation of chronic lymphocytic leukemia to Richter syndrome

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Activation of PI3K/Akt and MAPK pathways regulates Myc-mediated transcription by phosphorylating and promoting the degradation of Mad1

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Mnt, a novel Max-interacting protein is coexpressed with Myc in proliferating cells and mediates repression at Myc binding sites.Preprint

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Metabolic gatekeeper function of B-lymphoid transcription factors

Chan, L. N., Chen, Z., Braas, D., Lee, J. W., Xiao, G., Geng, H., Cosgun, K. N., Hurtz, C., Shojaee, S., Cazzaniga, V., et al. (2017) · Nature · doi:10.1038/nature21076 · Cited by 243 · see citing works

Structural perspective of cooperative transcription factor binding

Morgunova, E. Y., & Taipale, J. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.03.006 · Cited by 242 · see citing works

MYC and tumor metabolism: chicken and egg

Dejure, F. R., & Eilers, M. (2017) · The EMBO Journal · doi:10.15252/embj.201796438 · Cited by 240 · see citing works

Enhancer invasion shapes MYCN-dependent transcriptional amplification in neuroblastoma

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Myc-Nick: A Cytoplasmic Cleavage Product of Myc that Promotes α-Tubulin Acetylation and Cell Differentiation

Conacci‐Sorrell, M., Ngouenet, C., & Eisenman, R. N. (2010) · Cell · doi:10.1016/j.cell.2010.06.037 · Cited by 219 · see citing works

Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.Preprint

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Metabolic reprogramming in triple-negative breast cancer through Myc suppression of TXNIP

Shen, L., O’Shea, J. M., Kaadige, M. R., Cunha, S., Wilde, B. R., Cohen, A. L., Welm, A. L., & Ayer, D. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501555112 · Cited by 212 · see citing works

Deregulated Myc Requires MondoA/Mlx for Metabolic Reprogramming and Tumorigenesis

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High-resolution genomic profiling of chronic lymphocytic leukemia reveals new recurrent genomic alterations

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Mga, a dual‐specificity transcription factor that interacts with Max and contains a T‐domain DNA‐binding motif

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Functional antagonism between E2F family membersPreprint

Frolov, M. V., Huen, D. S., Nolan-Stevaux, O., Dimova, D. K., Balczarek-Strang, K., Elsdon, M. J., & Dyson, N. J. (2001) · Genes & Development · doi:10.1101/gad.903901 · Cited by 168 · see citing works

MAX Inactivation in Small Cell Lung Cancer Disrupts MYC–SWI/SNF Programs and Is Synthetic Lethal with BRG1

Romero, O. A., Torres-Diz, M., Pros, E., Savola, S. P., Gómez, A., Morán, S., Sáez, C., Iwakawa, R., Villanueva, A., Montuenga, L. M., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0799 · Cited by 164 · see citing works

Different promoter affinities account for specificity in MYC-dependent gene regulation

Lorenzin, F., Benary, U., Baluapuri, A., Walz, S., Jung, L. A., von Eyß, B., Kisker, C., Wolf, J., Eilers, M., & Wolf, E. (2016) · eLife · doi:10.7554/elife.15161 · Cited by 162 · see citing works

Combinatorial regulation of neuroblastoma tumor progression by N-Myc and hypoxia inducible factor HIF-1α

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Proteins Encoded by the Human c-myc Oncogene: Differential Expression in Neoplastic Cells

Hann, S., & Eisenman, R. N. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.11.2486-2497.1984 · Cited by 143 · see citing works

PCGF6-PRC1 suppresses premature differentiation of mouse embryonic stem cells by regulating germ cell-related genes

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Taming of the beast: shaping Myc-dependent amplification

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MondoA, a Novel Basic Helix-Loop-Helix–Leucine Zipper Transcriptional Activator That Constitutes a Positive Branch of a Max-Like Network

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Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non‐canonical E box and acts as a transcriptional repressor

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Inhibition of Cell Proliferation by the Mad1 Transcriptional Repressor

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Suppression of Myc, but not E1a, transformation activity by Max-associated proteins, Mad and Mxi1.

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CircadiOmics: integrating circadian genomics, transcriptomics, proteomics and metabolomics

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MondoA-Mlx Heterodimers Are Candidate Sensors of Cellular Energy Status: Mitochondrial Localization and Direct Regulation of Glycolysis

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Fructose 2,6-bisphosphate is essential for glucose-regulated gene transcription of glucose-6-phosphatase and other ChREBP target genes in hepatocytes

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Genomically complex lymphomas undergo sustained tumor regression upon MYC inactivation unless they acquire novel chromosomal translocations

Karlsson, A. E., Giuriato, S., Tang, F. L. M., Weier, J. F., Levan, G., & Felsher, D. W. (2003) · Blood · doi:10.1182/blood-2002-10-3091 · Cited by 116 · see citing works

Functional interactions among members of the MAX and MLX transcriptional network during oncogenesis

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The Role of MIZ-1 in MYC-Dependent TumorigenesisPreprint

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Mondo-Mlx Mediates Organismal Sugar Sensing through the Gli-Similar Transcription Factor Sugarbabe

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Mondo/ChREBP-Mlx-Regulated Transcriptional Network Is Essential for Dietary Sugar Tolerance in Drosophila

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Basic helix-loop-helix transcription factor gene family phylogenetics and nomenclature

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Myc/Mycn-mediated glycolysis enhances mouse spermatogonial stem cell self-renewalPreprint

Kanatsu‐Shinohara, M., Tanaka, T. S. T., Ogonuki, N., Ogura, A., Morimoto, H., Cheng, P. F., Eisenman, R. N., Trumpp, A., & Shinohara, T. (2016) · Genes & Development · doi:10.1101/gad.287045.116 · Cited by 104 · see citing works

Downregulation of c-MYC Protein Levels Contributes to Cancer Cell Survival under Dual Deficiency of Oxygen and Glucose

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Solution Structure of the Interacting Domains of the Mad–Sin3 Complex

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The ins and outs of virulence gene expression: Mg2 as a regulatory signal

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