Myc and Max associate in vivo
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It is shown here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max.Abstract:
Max is a helix-loop-helix zipper protein that associates in vitro with Myc family proteins to form a sequence-specific DNA-binding complex. We show here, by means of a coimmunoprecipitation assay with anti-Myc and anti-Max antibodies, that Myc and Max are associated in vivo and essentially all of the newly synthesized Myc can be detected in a complex with Max. This complex possesses specific DNA-binding activity for CACGTG-containing oligonucleotides. Although Max itself is a highly stable protein, Myc is rapidly degraded during or after its association with Max. In vivo Max is shown to be a nuclear protein phosphorylated by casein kinase II, and alternatively spliced forms of Max are expressed in cells. Furthermore, the levels of Max expression are equivalent in quiescent, mitogen-stimulated, and cycling cells. We conclude that the highly regulated rate of Myc biosynthesis is likely to be a limiting step in the formation of Myc:Max complexes.read more
Citations
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Journal ArticleDOI
Transcriptional Amplification in Tumor Cells with Elevated c-Myc
Charles Y. Lin,Jakob Lovén,Peter B. Rahl,Ronald M. Paranal,Christopher B. Burge,James E. Bradner,Tong Ihn Lee,Richard A. Young +7 more
TL;DR: It is reported here that in tumor cells expressing high levels of c-Myc the transcription factor accumulates in the promoter regions of active genes and causes transcriptional amplification, producing increased levels of transcripts within the cell's gene expression program.
Journal ArticleDOI
The Myc/Max/Mad Network and the Transcriptional Control of Cell Behavior
TL;DR: The Myc/Max/Mad network comprises a group of transcription factors whose distinct interactions result in gene-specific transcriptional activation or repression and can be viewed as a functional module which acts to convert environmental signals into specific gene-regulatory programs.
Journal ArticleDOI
Transcriptional regulation and transformation by Myc proteins
Sovana Adhikary,Martin Eilers +1 more
TL;DR: A wealth of data has shed new light on the biochemical functions of Myc proteins and on the mechanisms through which they function in cellular transformation.
Journal ArticleDOI
Histone Deacetylases Associated with the mSin3 Corepressor Mediate Mad Transcriptional Repression
TL;DR: It is proposed that Mad-Max functions by recruiting the mSin3-HDAC corepressor complex that deacetylates nucleosomal histones, producing alterations in chromatin structure that block transcription.
Journal ArticleDOI
Mxi1, a protein that specifically interacts with Max to bind Myc-Max recognition sites
TL;DR: A novel human protein that specifically interacts with Max, Mxi1, contains a bHLH-Zip motif that is simillar to that found in Myc family proteins, which is consistent with a model in which Mxi2-Max heterodimers indirectly inhibit Myc function in two ways.
References
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TL;DR: A new method of total RNA isolation by a single extraction with an acid guanidinium thiocyanate-phenol-chloroform mixture is described, providing a pure preparation of undegraded RNA in high yield and can be completed within 4 h.
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Journal ArticleDOI
The protein Id: A negative regulator of helix-loop-helix DNA binding proteins
Robert Benezra,Robert L. Davis,Robert L. Davis,Daniel Lockshon,David L. Turner,Harold Weintraub +5 more
TL;DR: It is proposed that HLH proteins lacking a basic region may negatively regulate other HLHprotein through the formation of nonfunctional heterodimeric complexes.
Journal ArticleDOI
Cell-Specific Regulation of the c-myc Gene by Lymphocyte Mitogens and Platelet-Derived Growth Factor
TL;DR: A regulatory linkage between the function of two oncogenes--c-myc and c-sis--the latter being the putative structural gene for PDGF is suggested, consistent with a model that a labile protein may regulate c- myc levels in these cells.
PatentDOI
Max: a helix-loop-helix zipper protein that forms a sequence-specific dna-binding complex with myc and mad
TL;DR: In this paper, the Max polypeptide when associated with the Myc or Mad polyPEptide is capable of binding to nucleotide sequences containing CACGTG.