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Mutual regulation of c-Jun and ATF2 by transcriptional activation and subcellular localization

Han Liu1, Xuehong Deng, Y John Shyu

  • 1Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.

The EMBO Journal
|March 3, 2006
PubMed

Insights

Activating protein-1 (AP-1) components ATF2 and c-Jun regulate gene expression. Nuclear localization of ATF2, controlled by c-Jun, is crucial for activating target genes like c-jun.

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Transcription Regulation

Background:

  • Activating protein-1 (AP-1) transcription factors, ATF2 and c-Jun, form dimers that regulate gene expression.
  • Previous understanding suggested constitutive nuclear localization for c-Jun and ATF2 activation by MAPKs.
  • Mechanisms governing AP-1 transcriptional activity regulation remained incompletely defined.

Purpose of the Study:

  • To elucidate the molecular mechanisms regulating ATF2 and c-Jun transcriptional activities.
  • To investigate the role of subcellular localization in AP-1 function.
  • To determine how ATF2 and c-Jun mutually regulate each other's localization and activity.

Main Methods:

  • Analysis of ATF2 nuclear localization signals (NLS) and nuclear export signal (NES).
  • Investigation of ATF2-c-Jun heterodimerization and its effect on ATF2 localization.
  • Observation of ATF2 localization during retinoic acid-induced differentiation and UV-induced cell death in F9 cells.

Main Results:

  • ATF2 shuttles continuously between the cytoplasm and nucleus due to identified NLS and NES.
  • Dimerization with c-Jun in the nucleus sequesters ATF2, preventing its export and enabling c-jun promoter activation.
  • c-Jun-dependent nuclear localization of ATF2 is observed during cellular differentiation and stress responses.

Conclusions:

  • ATF2 and c-Jun exhibit dynamic subcellular localization, regulated by their interaction.
  • Mutual regulation of localization and transcriptional activity is key to AP-1 function.
  • This study reveals a novel mechanism of transcriptional control through dynamic protein localization.

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