title: Phosphorylation of serum response factor, a factor that binds to the serum response element of the c-FOS enhancer.
abstract: Serum and growth factor regulation of c-FOS protooncogene transcription is mediated by the serum response element. A factor, serum response factor, binding to this element has already been identified. We demonstrate that serum response factor is phosphorylated in vivo on serine residues and that phosphatase treatment of this factor in vitro abolishes its DNA-binding activity. These results show phosphorylation of serum response factor to be required for its DNA-binding activity. The importance of serum response factor phosphorylation for the regulation of c-FOS expression is discussed.
authors.affiliation: Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.
authors.forename: R
authors.initials: R
authors.lastname: Prywes
authors.forename: A
authors.initials: A
authors.lastname: Dutta
authors.forename: J A
authors.initials: JA
authors.lastname: Cromlish
authors.forename: R G
authors.initials: RG
authors.lastname: Roeder
mesh_terms: D000818:Animals; D002460:Cell Line; D004247:DNA / Q000378:metabolism; D004742:Enhancer Elements, Genetic; D005786:Gene Expression Regulation; D006801:Humans; D009687:Nuclear Proteins / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D011519:Proto-Oncogenes; D026362:Serum Response Factor; D014158:Transcription, Genetic
chemical_list: D009687:Nuclear Proteins; D026362:Serum Response Factor; D004247:DNA; D010744:Phosphoric Monoester Hydrolases