Research Article1 March 1995free access ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. H. Gille H. Gille Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author M. Kortenjann M. Kortenjann Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author O. Thomae O. Thomae Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author C. Moomaw C. Moomaw Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author C. Slaughter C. Slaughter Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author M.H. Cobb M.H. Cobb Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author P.E. Shaw P.E. Shaw Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author H. Gille H. Gille Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author M. Kortenjann M. Kortenjann Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author O. Thomae O. Thomae Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author C. Moomaw C. Moomaw Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author C. Slaughter C. Slaughter Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author M.H. Cobb M.H. Cobb Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author P.E. Shaw P.E. Shaw Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. Search for more papers by this author Author Information H. Gille1, M. Kortenjann1, O. Thomae1, C. Moomaw1, C. Slaughter1, M.H. Cobb1 and P.E. Shaw1 1Max-Planck-Institut für Immunbiologie, Spemann Laboratories, Freiburg, Germany. The EMBO Journal (1995)14:951-962https://doi.org/10.1002/j.1460-2075.1995.tb07076.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Induction of the human c-fos proto-oncogene by mitogens depends on the formation of a ternary complex by p62TCF with the serum response factor (SRF) and the serum response element (SRE). We demonstrate that Elk-1, a protein closely related to p62TCF in function, is a nuclear target of two members of the MAP kinase family, ERK1 and ERK2. Phosphorylation of Elk-1 increases the yield of ternary complex in vitro. At least five residues in the C-terminal domain of Elk-1 are phosphorylated upon growth factor stimulation of NIH3T3 cells. These residues are also phosphorylated by purified ERK1 in vitro, as determined by a combination of phosphopeptide sequencing and 2-D peptide mapping. Conversion of two of these phospho-acceptor sites to alanine impairs the formation of ternary complexes by the resulting Elk-1 proteins. Removal of these serine residues also drastically diminishes activation of the c-fos promoter in epidermal growth factor-treated cells. Analogous mutations at other sites impair activation to a lesser extent without affecting ternary complex formation in vitro. Our results indicate that phosphorylation regulates ternary complex formation by Elk-1, which is a prerequisite for the manifestation of its transactivation potential at the c-fos SRE. Previous ArticleNext Article Volume 14Issue 51 March 1995In this issue RelatedDetailsLoading ...