HSV-1 ICP27 induces apoptosis by promoting Bax translocation to mitochondria through interacting with 14-3-3θ

BMB Rep. 2017 May;50(5):257-262. doi: 10.5483/bmbrep.2017.50.5.023.

Abstract

The subcellular localization of Bax plays a crucial role during apoptosis. In response to apoptotic stimuli, Bax translocates from the cytoplasm to the mitochondria, where it promotes the release of cytochrome c to the cytoplasm. In cells infected with HSV-1, apoptosis is triggered or blocked by diverse mechanisms. In this study, we demonstrate how HSV-1 ICP27 induces apoptosis and modulates mitochondrial membrane potential in HEK 293T cells. We found that ICP27 interacts with 14-3-3θ which sequesters Bax to the cytoplasm. In addition, ICP27 promotes the translocation of Bax to the mitochondria by inhibiting the interaction between 14-3-3θ and Bax. Our findings may provide a novel apoptotic regulatory pathway induced by ICP27 during HSV-1 infection. [BMB Reports 2017; 50(5): 257-262].

MeSH terms

  • 14-3-3 Proteins / genetics
  • 14-3-3 Proteins / metabolism*
  • Apoptosis / genetics
  • Apoptosis / physiology
  • Carrier Proteins / metabolism
  • Caspases / metabolism
  • Cytochromes c / metabolism
  • Cytoplasm
  • HEK293 Cells
  • Herpesvirus 1, Human
  • Humans
  • Immediate-Early Proteins / metabolism*
  • Mitochondria
  • Protein Translocation Systems / metabolism
  • Protein Translocation Systems / physiology
  • Proto-Oncogene Proteins / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / metabolism
  • bcl-2-Associated X Protein / metabolism*

Substances

  • 14-3-3 Proteins
  • Carrier Proteins
  • ICP27 protein, human herpesvirus 1
  • Immediate-Early Proteins
  • Protein Translocation Systems
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-bcl-2
  • bcl-2-Associated X Protein
  • Cytochromes c
  • Caspases