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Cleavage and cytoplasmic relocalization of histone deacetylase 3 are important for apoptosis progression

Fabrice Escaffit1, Olivier Vaute, Martine Chevillard-Briet

  • 1Laboratoire de Biologie Moléculaire Eucaryote, UMR5099, CNRS and Université Paul Sabatier, IFR109, 118 Route de Narbonne, 31062 Toulouse Cedex 4, France.

Molecular and Cellular Biology
|November 15, 2006
PubMed

Insights

Histone deacetylase 3 (HDAC-3) cleavage during apoptosis is caspase-dependent and crucial for activating proapoptotic genes. This process, involving cytoplasmic relocalization, enhances histone acetylation and gene expression for efficient cell death.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Apoptosis involves significant alterations in chromatin structure and gene expression.
  • The apoptotic genetic program regulates the balance between antiapoptotic and proapoptotic genes.
  • Histone deacetylase 3 (HDAC-3) functions as a co-repressor for numerous proapoptotic genes.

Purpose of the Study:

  • To investigate the role and mechanism of histone deacetylase 3 (HDAC-3) cleavage during apoptosis.
  • To determine the functional significance of HDAC-3 cleavage and its subcellular localization in apoptosis induction.

Main Methods:

  • Analysis of HDAC-3 proteolytic cleavage during apoptosis across different cell types and species.
  • Investigation of caspase dependency and the consequences of HDAC-3 cleavage on its localization.
  • Assessment of HDAC-3's impact on histone acetylation and target gene expression, specifically the Fas gene.

Main Results:

  • HDAC-3 undergoes caspase-dependent proteolytic cleavage during apoptosis, independent of cell type and species.
  • Cleavage results in the loss of HDAC-3's C-terminal portion and its accumulation in the cytoplasm.
  • Forced nuclear localization of HDAC-3 impairs apoptosis, while cytoplasmic relocalization is vital for the process; cleavage increases histone acetylation and activates proapoptotic Fas gene expression.

Conclusions:

  • HDAC-3 cleavage is a critical event in efficient apoptosis induction.
  • Cytoplasmic relocalization of cleaved HDAC-3 facilitates the activation of proapoptotic genes, such as Fas.
  • This mechanism highlights a novel role for HDAC-3 processing in regulating gene expression during programmed cell death.

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