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dc.contributor.authorSeth, Alpna
dc.contributor.authorAlvarez, Elvira
dc.contributor.authorGupta, Shashi
dc.contributor.authorDavis, Roger J.
dc.date2022-08-11T08:08:48.000
dc.date.accessioned2022-08-23T16:08:46Z
dc.date.available2022-08-23T16:08:46Z
dc.date.issued1991-12-15
dc.date.submitted2008-12-10
dc.identifier.citation<p>J Biol Chem. 1991 Dec 15;266(35):23521-4.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid1748630
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32530
dc.description.abstractThe c-myc gene encodes a sequence-specific DNA-binding protein (c-Myc) that forms leucine zipper complexes and can act as a transcription factor. Growth factor stimulation of cells causes the phosphorylation of the c-Myc transcriptional activation domain at Ser62 within a proline-rich region that is highly conserved among members of the Myc family (Alvarez, E., Northwood, I.C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T., and Davis, R. J. (1991) J. Biol. Chem. 266, 15277-15285). This phosphorylation site is a substrate for growth factor-regulated MAP kinases and for the cell cycle-dependent protein kinase p34cdc2. We report that serum treatment of cells results in a marked increase in the transactivation of gene expression mediated by the c-Myc transcriptional activation domain. A point mutation at the site of growth factor-stimulated phosphorylation (Ser62) decreases the serum induction of transactivation. These data indicate that the c-Myc transcriptional activation domain may be a direct target of signal transduction pathways.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=1748630&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttp://www.jbc.org/content/266/35/23521.short
dc.subjectAmino Acid Sequence; Animals; CHO Cells; Chloramphenicol O-Acetyltransferase; Cricetinae; Gene Expression; Gene Expression Regulation; Hela Cells; Humans; Mutagenesis, Insertional; Phosphorylation; Plasmids; Proto-Oncogene Proteins c-myc; *Trans-Activation (Genetics); Transcription, Genetic; Transfection
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume266
dc.source.issue35
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1097
dc.identifier.contextkey679635
html.description.abstract<p>The c-myc gene encodes a sequence-specific DNA-binding protein (c-Myc) that forms leucine zipper complexes and can act as a transcription factor. Growth factor stimulation of cells causes the phosphorylation of the c-Myc transcriptional activation domain at Ser62 within a proline-rich region that is highly conserved among members of the Myc family (Alvarez, E., Northwood, I.C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T., and Davis, R. J. (1991) J. Biol. Chem. 266, 15277-15285). This phosphorylation site is a substrate for growth factor-regulated MAP kinases and for the cell cycle-dependent protein kinase p34cdc2. We report that serum treatment of cells results in a marked increase in the transactivation of gene expression mediated by the c-Myc transcriptional activation domain. A point mutation at the site of growth factor-stimulated phosphorylation (Ser62) decreases the serum induction of transactivation. These data indicate that the c-Myc transcriptional activation domain may be a direct target of signal transduction pathways.</p>
dc.identifier.submissionpathgsbs_sp/1097
dc.contributor.departmentProgram in Molecular Medicine
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages23521-4


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