The Myc:Max Protein Complex and Cell Growth Regulation

Blackwood, Elizabeth M.; Lüscher, Bernhard; Kretzner, Leo; Eisenman, R N

doi:10.1101/sqb.1991.056.01.015

Cited by 41 publications

(24 citation statements)

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“…The N-terminal domain consists of the transcriptional activation domain, whereas the C-terminal domain mediates DNA binding to promoters of target genes. In recent years, many new C-terminal domain-and N-terminal domain-interacting proteins have been identified (34,35).…”

Section: Kaposi Sarcoma-associated Herpes Virus (Kshv)mentioning

confidence: 99%

Stimulation of c-Myc Transcriptional Activity by vIRF-3 of Kaposi Sarcoma-associated Herpesvirus

Lubyová

Kellum

Frisancho

et al. 2007

Journal of Biological Chemistry

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Section: Kaposi Sarcoma-associated Herpes Virus (Kshv)mentioning

confidence: 99%

Stimulation of c-Myc Transcriptional Activity by vIRF-3 of Kaposi Sarcoma-associated Herpesvirus

Lubyová

Kellum

Frisancho

et al. 2007

Journal of Biological Chemistry

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“…However, the underlying molecular mechanism(s) responsible for c-Myc-induced tumorigenesis remains elusive. Human cMyc is a 439-amino-acid protein that when bound to its partner, Max, can interact with DNA and function as a transcription factor (4). Myc-Max heterodimerization, which occurs through the interaction of C-terminal basic helix-loop-helix and leucine zipper motifs, is required for virtually all wellknown c-Myc-associated phenotypes: cell proliferation, growth, transformation, and apoptosis (9,15).…”

mentioning

confidence: 99%

Overexpression of c-Myc Alters G₁/S Arrest following Ionizing Radiation

Sheen

Dickson

2002

Molecular and Cellular Biology

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Study of the mechanism(s) of genomic instability induced by the c-myc proto-oncogene has the potential to shed new light on its well-known oncogenic activity. However, an underlying mechanism(s) for this phenotype is largely unknown. In the present study, we investigated the effects of c-Myc overexpression on the DNA damage-induced G 1 /S checkpoint, in order to obtain mechanistic insights into how deregulated c-Myc destabilizes the cellular genome. The DNA damage-induced checkpoints are among the primary safeguard mechanisms for genomic stability, and alterations of cell cycle checkpoints are known to be crucial for certain types of genomic instability, such as gene amplification. The effects of c-Myc overexpression were studied in human mammary epithelial cells (

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“…U937 cells are a good model system for studying myeloid differentiation in general, as they are bipotential and can be differentiated into granulocytic lineage by RA and in particular, with respect to the functions of C/EBPa, as a threefold level of C/EBPa protein (above the level of endogenous C/EBPa) in U937 cells is sufficient for their granulocytic differentiation. 26 In addition to nine other proteins (see Table), we identified Max, an essential heterodimerization partner of Myc, 16 as a novel interacting partner of C/EBPa in our screen (Figure 1). The discovery of Max as a novel C/EBPa partner is intriguing because of the role Max plays in switching of the complexes during myeloid differentiation.…”

Section: Daymentioning

confidence: 99%

“…[12][13][14][15] Max can form a homo-or a heterodimer and bind specifically to E-box DNA elements in target promoters (consensus CACGTG). 16,17 To function as transcriptional regulators, the members of the Myc and Mad families must heterodimerize with Max. Whereas Myc-Max activates transcription, Mad-Max and Mnt-Max repress transcription.…”

Section: Introductionmentioning

confidence: 99%

Proteomic discovery of Max as a novel interacting partner of C/EBPα: a Myc/Max/Mad link

et al. 2006

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The transcription factor CCAAT/enhancer binding protein a (C/EBPa) is important in the regulation of granulopoiesis and is disrupted in human acute myeloid leukemia. In the present study, we sought to identify novel C/EBPa interacting proteins in vivo through immunoprecipitation using mass spectrometrybased proteomic techniques. We identified Max, a heterodimeric partner of Myc, as one of the interacting proteins of C/EBPa in our screen. We confirmed the in vivo interaction of C/EBPa with Max and showed that this interaction involves the basic region of C/EBPa. Endogenous C/EBPa and Max, but not Myc and Max, colocalize in intranuclear structures during granulocytic differentiation of myeloid U937 cells. Max enhanced the transactivation capacity of C/EBPa on a minimal promoter. A chromatin immunoprecipitation assay revealed occupancy of the human C/EBPa promoter in vivo by Max and Myc under cellular settings and by C/EBPa and Max under retinoic acid induced granulocytic differentiation. Interestingly, enforced expression of Max and C/EBPa results in granulocytic differentiation of the human hematopoietic CD34 þ cells, as evidenced by CD11b, CD15 and granulocyte colony-stimulating factor receptor expression. Silencing of Max by short hairpin RNA in CD34 þ and U937 cells strongly reduced the differentiation-inducing potential of C/EBPa, indicating the importance of C/EBPa-Max in myeloid progenitor differentiation. Taken together, our data reveal Max as a novel co-activator of C/EBPa functions, thereby suggesting a possible link between C/EBPa and Myc-Max-Mad network.

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The Myc:Max Protein Complex and Cell Growth Regulation

Cited by 41 publications

References 0 publications

Stimulation of c-Myc Transcriptional Activity by vIRF-3 of Kaposi Sarcoma-associated Herpesvirus

Stimulation of c-Myc Transcriptional Activity by vIRF-3 of Kaposi Sarcoma-associated Herpesvirus

Overexpression of c-Myc Alters G₁/S Arrest following Ionizing Radiation

Proteomic discovery of Max as a novel interacting partner of C/EBPα: a Myc/Max/Mad link

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The Myc:Max Protein Complex and Cell Growth Regulation

Cited by 41 publications

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Stimulation of c-Myc Transcriptional Activity by vIRF-3 of Kaposi Sarcoma-associated Herpesvirus

Stimulation of c-Myc Transcriptional Activity by vIRF-3 of Kaposi Sarcoma-associated Herpesvirus

Overexpression of c-Myc Alters G1/S Arrest following Ionizing Radiation

Proteomic discovery of Max as a novel interacting partner of C/EBPα: a Myc/Max/Mad link

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Overexpression of c-Myc Alters G₁/S Arrest following Ionizing Radiation