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J. Biol. Chem., Vol. 266, Issue 35, 23521-23524, Dec, 1991
A Seth, E Alvarez, S Gupta and RJ Davis
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.
A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression
Program in Molecular Medicine, University of Massachusetts Medical School, Worcester 01605.
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