<i>myc</i> FUNCTION AND REGULATION

Marcu, Kenneth B.; Bossone, Steven A.; Patel, Amanda

doi:10.1146/annurev.bi.61.070192.004113

Cited by 791 publications

(633 citation statements)

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“…Since the E-box found in the Gp-LCR is CACGTG which is the consensus binding site for Max/Max and Myc/Max (Ho man-Liberman and Liberman, 1991; Dunn et al, 1994;Larsson et al, 1994;Marcu et al, 1992), it is possible that c-Myc/Max can bind to the E-box, but, addition of the anti c-Myc antibody neither reduced nor supershifted the band with EY as shown in Figure 1a. A mutation in the YY-1 binding site (EDY) did not cause resumption of ca b Figure 8 DNase I footprinting and methylation interference assay.…”

Section: Discussionmentioning

confidence: 96%

“…c-Myc is a basic-helix ± loop ± helix-zipper (bHLHZip) nuclear oncoprotein that heterodimerizes with Max, another bHLHZip protein, to exert its functions as both a speci®c DNA binding transcriptional activator and a transforming protein by binding to the speci®c DNA sequence E-box (CACGTG) (Ho man-Liberman and Liberman, 1991; Dunn et al, 1994;Larsson et al, 1994;Marcu et al, 1992). In addition, downregulation of c-Myc is important for induction of di erentiation of MEL cells a b c Figure 7 EMSA with EY oligonucleotides.…”

Section: Discussionmentioning

confidence: 99%

“…To learn the combinatorial mechanism of YY-1 and EBP, the binding of both proteins on the Gp-LCR was examined. Since the E-box found in the GP-LCR is CACGTG which is the consensus binding site for Max/Max and Myc/Max (Ho man-Liberman and Liberman, 1991; Dunn et al, 1994;Larsson et al, 1994;Marcu et al, 1992), it is possible that c-Myc/Max can bind to the E-box, but, addition of the anti c-Myc antibody neither reduced nor supershifted the band with EY as shown in Figure 1a. Because it is possible that binding of YY-1 sterically inhibited the E-box binding site, EMSA was performed with the EDY.…”

Section: Combinatorial Binding Of Yy-1 and Ebp To The Gp-lcrmentioning

confidence: 96%

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Direct association of YY-1 with c-Myc and the E-box binding protein in regulation of glycophorin gene expression

et al. 1998

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We previously reported that YY-1, a versatile transcription factor, regulates expression of glycophorin gene by binding to its locus control region-like region (Gp-LCR) in combination with E-box binding protein during murine erythroleukemia (MEL) cell di erentiation. In the present work, we demonstrated that YY-1 and c-Myc, a nuclear oncoprotein, were physically associated in vivo and that down regulation of c-Myc liberated free YY-1 from its complex, resulting in the functional binding of YY-1 to the Gp-LCR. We also showed that the E-box binding protein (EBP) which bound to E-box was physically associated with YY-1, facilitated binding of YY-1 to the neighboring site and their combinatorial binding may stimulate the GpLCR mediated enhancement of erythroid-speci®c transcription of glycophorin gene in MEL cells.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Combinatorial Binding Of Yy-1 and Ebp To The Gp-lcrmentioning

confidence: 96%

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Direct association of YY-1 with c-Myc and the E-box binding protein in regulation of glycophorin gene expression

et al. 1998

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“…The c-myc oncoprotein, member of the basic helix ± loop ± helix ± leucine zippr (bHLH-ZIP) family, plays important roles in proliferation, di erentiation, transformation, and apoptosis (DePinho et al, 1990;Askew et al, 1991;Marcu et al, 1992;Evan et al, 1992Evan et al, , 1994Evan and Littlewood, 1993;Amati and Land, 1994). Cmyc is a DNA binding protein whose recognition site, CACGTG, conforms to the consensus E-box element (CANNTG) bound by other bHLH-ZIP proteins as well as the larger category of proteins lacking leucine zipper domains (the bHLH proteins) Halazonetis and Kandil, 1991;Kerkho et al, 1991;.…”

Section: Introductionmentioning

confidence: 99%

Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc

et al. 1998

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C-myc, a member of the basic helix ± loop ± helix ± leucine zipper (bHLH-ZIP) protein family activates target genes in heterodimeric association with another bHLH-ZIP protein, Max. Max readily homodimerizes, competes with C-myc-Max heterodimers, and represses transcription. Four additional bHLH-ZIP proteins, Mad1, Mxi1, Mad3 and Mad4, heterodimerize with Max and also repress transcription of c-myc-responsive genes. We employed a yeast two-hybid approach to identify proteins which interact with Mxi. We identi®ed a novel ZIP-containing protein, Mmip1 (Mad memberinteracting protein 1) that strongly dimerizes with all four Mad members, but not with c-myc, Max, or with unrelated HLH proteins. The Mmip1-Mxi association is mediated by the ZIP domain of each polypeptide and is as strong or stronger than the associations between cmyc and Max or Max and Mxi1. In vitro, Mmip1 can inhibit DNA binding by Max-Mad heterodimers and, in vivo, can reverse the suppressive e ects of Mad proteins on c-myc functions. Mmip1 is found in a variety of cells types, is induced by serum stimulation, and can be coimmunoprecipitated from ®broblasts in association with Mxi1. By interfering with the dimerization between Max and Mad family member proteins, Mmip1 can indirectly up-regulate the transcriptional activity of c-myc and suppress the antiproliferative actions of Mad proteins.

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“…[1][2][3] The importance of cmyc in mammary tumorigenesis was first identified in transgenic mouse models. 4 In human breast carcinomas, genetic abnormalities including c-myc amplification, rearrangement and overexpression have been widely reported.…”

mentioning

confidence: 99%

C‐myc gene expression alone is sufficient to confer resistance to antiestrogen in human breast cancer cells

Venditti

Iwasiow

Orr

et al. 2002

Intl Journal of Cancer

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myc FUNCTION AND REGULATION

Cited by 791 publications

References 1 publication

Direct association of YY-1 with c-Myc and the E-box binding protein in regulation of glycophorin gene expression

Direct association of YY-1 with c-Myc and the E-box binding protein in regulation of glycophorin gene expression

Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc

C‐myc gene expression alone is sufficient to confer resistance to antiestrogen in human breast cancer cells

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