Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

Amino-acid substitutions modulate the effect of jun on transformation, transcriptional activation and DNA-replication

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Morgan, I. M.
  • Asano, M.
  • Havarstein, L. S.
  • Ishikawa, H.
  • Hiiragi, T.
  • Ito, Y.
  • Vogt, Peter K.

publication date

  • May 1993

journal

  • Oncogene  Journal

abstract

  • The retroviral oncogene v-jun and its cellular counterpart code for proteins that function as major components of the transcription factor complex AP-1. Jun proteins bind to the AP-1 consensus sequence as homodimers or heterodimers with members of the Fos protein family. This report compares the ability of viral and cellular Jun proteins (v-Jun and c-Jun) to activate transcription and to stimulate DNA synthesis. The effect of amino acid substitutions on cellular transformation is also described. In F9 cells c-Jun is a more effective transactivator than v-Jun, which carries two amino acid substitutions in the carboxy-terminal region that together down-regulate transactivation. The delta deletion, present in the amino-terminal region of v-Jun, does not affect transactivation in F9 cells; however, it does modulate the stimulation of DNA synthesis. When delta is deleted, the amino acid substitutions are without consequence on DNA synthesis. In the presence of delta the amino acid substitutions down-regulate DNA synthesis. Deletion of the Jun transactivation domain, which is required for cellular transformation, abolishes both transactivation and stimulation of DNA synthesis. We conclude that transformation, transactivation and stimulation of DNA synthesis all depend on the presence of the transactivation domain. The three functions are, however, not tightly correlated, and further work is needed to define the role of the biochemical activities of Jun in oncogenesis.

subject areas

  • 3T3 Cells
  • Animals
  • Base Sequence
  • Cell Transformation, Neoplastic
  • Chick Embryo
  • DNA
  • DNA Replication
  • Female
  • Mice
  • Molecular Sequence Data
  • Oncogene Protein p65(gag-jun)
  • Proto-Oncogene Proteins c-jun
  • Structure-Activity Relationship
  • Transcriptional Activation
  • Transfection
  • Tumor Cells, Cultured
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0950-9232

PubMed ID

  • 8479738
scroll to property group menus

Additional Document Info

start page

  • 1135

end page

  • 1140

volume

  • 8

issue

  • 5

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support