Abstract
An amino-terminal transactivation domain is required for Myc to function as a transcription factor controlling cell proliferation, differentiation, and apoptosis. A complementary DNA expression library was screened with a Myc fusion protein to identify proteins interacting with this domain, and a clone encoding the Rb-related p107 protein was isolated. The p107 protein was shown to associate with Myc in vivo and to suppress the activity of the Myc transactivation domain. However, mutant forms of Myc from Burkitt lymphoma cells, which contain sequence alterations in the transactivation domain, were resistant to p107-mediated suppression. Thus, disruption of a regulatory interaction between Myc and p107 may be important in tumorigenesis.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3T3 Cells
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Animals
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Base Sequence
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Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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Basic-Leucine Zipper Transcription Factors
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DNA-Binding Proteins / metabolism
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Helix-Loop-Helix Motifs
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Lymphoma, B-Cell
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Mice
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Molecular Sequence Data
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Nuclear Proteins*
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Point Mutation
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Proteins / metabolism*
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Proto-Oncogene Proteins c-myc / genetics
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Proto-Oncogene Proteins c-myc / metabolism*
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Recombinant Fusion Proteins / metabolism
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Retinoblastoma-Like Protein p107
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Suppression, Genetic*
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Transcription Factors*
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Transcriptional Activation*
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Transfection
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Tumor Cells, Cultured
Substances
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Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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Basic-Leucine Zipper Transcription Factors
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DNA-Binding Proteins
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Myc associated factor X
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Nuclear Proteins
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Proteins
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Proto-Oncogene Proteins c-myc
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Rbl1 protein, mouse
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Recombinant Fusion Proteins
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Retinoblastoma-Like Protein p107
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Transcription Factors
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Max protein, mouse