| pubmed-article:1620120 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C0086661 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C0920487 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:1620120 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:1620120 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:1620120 | pubmed:dateCreated | 1992-8-6 | lld:pubmed |
| pubmed-article:1620120 | pubmed:abstractText | Members of the Myc family of proteins share a number of protein motifs that are found in regulators of gene transcription. Conserved stretches of amino acids found in the N-terminal transcriptional activation domain of c-Myc are required for cotransforming activity. Most of the Myc proteins contain the basic helix-loop-helix zipper (bHLH-Zip) DNA-binding motif which is also required for the cotransforming activity of c-Myc. L-Myc, the product of a myc family gene that is highly amplified in many human lung carcinomas, was found to cotransform primary rat embryo cells with an activated ras gene. However, L-Myc cotransforming activity was only 1 to 10% of that of c-Myc (M. J. Birrer, S. Segal, J. S. DeGreve, F. Kaye, E. A. Sausville, and J. D. Minna, Mol. Cell. Biol. 8:2668-2673, 1988). We sought to determine whether functional differences between c-Myc and L-Myc in either the N-terminal or the C-terminal domain could account for the relatively diminished L-Myc cotransforming activity. Although the N-terminal domain of L-Myc could activate transcription when fused to the yeast GAL4 DNA-binding domain, the activity was only 5% of that of a comparable c-Myc domain. We next determined that the interaction of the C-terminal bHLH-Zip region of L-Myc or c-Myc with that of a Myc partner protein, Max, was equivalent in transfected cells. A Max expression vector was found to augment the cotransforming activity of L-Myc as well as that of c-Myc. In addition, a bacterially synthesized DNA-binding domain of L-Myc, like that o c-Myc, heterodimerizes with purified Max protein to bind the core DNA sequence CACGTG. To determine the region of L-Myc responsible for its relatively diminished cotransforming activity, we constructed chimeras containing exons 2 (constituting activation domains) and 3 (constituting DNA-binding domains) of c-Myc fused to those of L-Myc. The cotransforming potencies of these chimeras were compared with those of full-length L-Myc of c-Myc in rat embryo cells. The relative cotransforming activities suggest that the potencies of the activation domains determine the cotransforming efficiencies for c-Myc and L-Myc. This correlation supports the hypothesis that the Myc proteins function in neoplastic cotransformation as transcription factors. | lld:pubmed |
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| pubmed-article:1620120 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1620120 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1620120 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1620120 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1620120 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1620120 | pubmed:issn | 0270-7306 | lld:pubmed |
| pubmed-article:1620120 | pubmed:author | pubmed-author:BarrettJJ | lld:pubmed |
| pubmed-article:1620120 | pubmed:author | pubmed-author:DangC VCV | lld:pubmed |
| pubmed-article:1620120 | pubmed:author | pubmed-author:Dosaka-AkitaH... | lld:pubmed |
| pubmed-article:1620120 | pubmed:author | pubmed-author:KatoG JGJ | lld:pubmed |
| pubmed-article:1620120 | pubmed:author | pubmed-author:BirrerM JMJ | lld:pubmed |
| pubmed-article:1620120 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1620120 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:1620120 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1620120 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1620120 | pubmed:pagination | 3130-7 | lld:pubmed |
| pubmed-article:1620120 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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