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Heterodimerization with Jun family members regulates c-Fos nucleocytoplasmic traffic

Cécile E Malnou1, Tamara Salem, Frédérique Brockly

  • 1Institut de Génétique Moléculaire de Montpellier, CNRS, UMR5535, 1919 Route de Mende, Montpellier F-34293, France.

The Journal of Biological Chemistry
|August 8, 2007
PubMed

Insights

The c-Fos proto-oncoprotein

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Oncogenesis

Background:

  • c-Fos proto-oncoprotein is a key component of AP-1 transcription factor complexes.
  • Its role in cell function and tumorigenesis is established, but its intracellular dynamics are poorly understood.

Purpose of the Study:

  • To investigate the intracellular distribution and nucleocytoplasmic shuttling of c-Fos.
  • To elucidate the role of dimerization in regulating c-Fos localization and function.

Main Methods:

  • Genetic approaches
  • Cell biology techniques
  • Microscopic imaging

Main Results:

  • A second, non-classic nuclear localization signal (NLS) dependent on transportin 1 was identified in c-Fos.
  • c-Fos undergoes Crm-1 exportin-independent nucleocytoplasmic shuttling.
  • Dimerization with Jun proteins, particularly c-Jun, inhibits c-Fos nuclear exit.
  • Monomeric Jun proteins actively shuttle, unlike dimeric forms.

Conclusions:

  • Dimerization is critical for maintaining AP-1 transcription complexes within the nucleus.
  • This regulation ensures AP-1 proteins remain in the compartment where they exert transcriptional functions.
  • The findings reveal a novel regulatory mechanism for AP-1 activity based on protein dimerization and localization.

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