Behind the Fos and Jun leucine zipper

Cancer Cells. 1989 Nov;1(3):71-6.

Abstract

The production of the nuclear oncoproteins Fos and Jun is rapidly induced in response to extracellular signals. In the nucleus, the two proteins combine to form a tight complex via leucine zipper domains. The resulting Fos-Jun heterodimer can bind to the TPA-responsive element (TRE) by way of a novel, highly basic motif and can activate the transcription of TPA-responsive genes. The existence of several Fos- and Jun-related proteins with dimerization and DNA binding properties similar to Fos and Jun suggests that these two oncoproteins may be part of a network of related but functionally distinct transcription factors.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • DNA / metabolism*
  • Leucine / metabolism*
  • Macromolecular Substances
  • Molecular Sequence Data
  • Oncogene Protein p65(gag-jun)
  • Oncogene Proteins v-fos
  • Oncogene Proteins, Viral / metabolism*
  • Retroviridae Proteins, Oncogenic / metabolism*
  • Transcription Factors / metabolism*

Substances

  • Macromolecular Substances
  • Oncogene Protein p65(gag-jun)
  • Oncogene Proteins v-fos
  • Oncogene Proteins, Viral
  • Retroviridae Proteins, Oncogenic
  • Transcription Factors
  • DNA
  • Leucine