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Abstract

The Myc oncoprotein dimerizes with its partner, Max, to bind DNA, activate transcription, and promote cell proliferation, as well as programmed cell death. Max also forms homodimers or heterodimers with its alternative partners, Mad and Mxi-1. These complexes behave as antagonists of Myc/Max through competition for common DNA targets, and perhaps permit cellular differentiation.

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Most cited references 37

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Induction of apoptosis in fibroblasts by c-myc protein

Gerard Evan, Andrew H. Wyllie, Christopher S. Gilbert … (1992)

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Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.

R Eisenman, Elizabeth Blackwood (1991)

The myc protooncogene family has been implicated in cell proliferation, differentiation, and neoplasia, but its mechanism of function at the molecular level is unknown. The carboxyl terminus of Myc family proteins contains a basic region helix-loop-helix leucine zipper motif (bHLH-Zip), which has DNA-binding activity and has been predicted to mediate protein-protein interactions. The bHLH-Zip region of c-Myc was used to screen a complementary DNA (cDNA) expression library, and a bHLH-Zip protein, termed Max, was identified. Max specifically associated with c-Myc, N-Myc, and L-Myc proteins, but not with a number of other bHLH, bZip, or bHLH-Zip proteins. The interaction between Max and c-Myc was dependent on the integrity of the c-Myc HLH-Zip domain, but not on the basic region or other sequences outside the domain. Furthermore, the Myc-Max complex bound to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibited appreciable binding. The DNA-binding activity of the complex was dependent on both the dimerization domain and the basic region of c-Myc. These results suggest that Myc family proteins undergo a restricted set of interactions in the cell and may belong to the more general class of eukaryotic DNA-binding transcription factors.

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

A. Ferre-D'Amare, G C Prendergast, E B Ziff … (1993)

The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.

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PubMed ID:: 8193530

DOI:: 10.1016/0959-437x(94)90098-1

ScienceOpen disciplines: Chemistry

Keywords: Animals,Apoptosis,physiology,Base Sequence,Basic Helix-Loop-Helix Leucine Zipper Transcription Factors,Basic-Leucine Zipper Transcription Factors,Binding Sites,Cell Cycle,Cell Differentiation,DNA,genetics,metabolism,DNA-Binding Proteins,Helix-Loop-Helix Motifs,Humans,Leucine Zippers,Proto-Oncogene Proteins c-myc,Repressor Proteins,Transcription Factors

Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death.

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Abstract

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Photoluminescent Nanomaterials

Most cited references 37

Induction of apoptosis in fibroblasts by c-myc protein

Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc.

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

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