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The antiapoptotic protein AAC-11 interacts with and regulates Acinus-mediated DNA fragmentation

Patricia Rigou1, Valeria Piddubnyak, Audrey Faye

  • 1INSERM UMRS 940, Equipe Avenir, Université Paris 7, Institut de Génétique Moléculaire, Paris, France.

The EMBO Journal
|April 24, 2009
PubMed

Insights

The survival protein AAC-11 binds to nuclear factor Acinus, preventing DNA fragmentation and protecting cells from apoptosis. Targeting AAC-11 may sensitize cancer cells to chemotherapy.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Nuclear factor Acinus is implicated in apoptotic chromatin condensation and DNA cleavage.
  • The precise role of Acinus in apoptosis requires further elucidation.
  • AAC-11 is a survival protein that inhibits apoptosis upon growth factor deprivation.

Purpose of the Study:

  • To investigate the interaction between AAC-11 and Acinus.
  • To determine the role of AAC-11 in Acinus-mediated DNA fragmentation.
  • To explore the potential of targeting AAC-11 for cancer therapy.

Main Methods:

  • In vivo and in vitro assays to study protein interactions and cleavage.
  • Assessment of cellular sensitivity to anticancer drugs upon AAC-11 modulation.
  • Use of cell-permeable peptides to disrupt AAC-11-Acinus complex formation.

Main Results:

  • AAC-11 directly binds to Acinus and prevents Acinus-mediated DNA fragmentation.
  • AAC-11 protects Acinus from caspase-3 cleavage, inhibiting its pro-apoptotic function.
  • AAC-11 depletion increases sensitivity to anticancer drugs, while its expression confers resistance.
  • Disruption of the AAC-11-Acinus complex potentiates drug-induced apoptosis in cancer cells.

Conclusions:

  • AAC-11 functions as a survival protein by inhibiting Acinus-mediated DNA fragmentation.
  • Targeting the AAC-11-Acinus interaction represents a potential strategy to enhance chemotherapy efficacy.
  • AAC-11 modulation offers a novel approach for sensitizing tumor cells to chemotherapeutic agents.

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