FEBS Letters
Volume 584, Issue 15 , Pages 3305-3310, 4 August 2010

Upregulation of Bcl2 inhibits apoptosis-driven BAX insertion but favors BAX relocalization in mitochondria

Edited by Quan Chen

  • O. Teijido
    • ,
  • L. Dejean

      Affiliations

    • Corresponding Author InformationCorresponding author. Address: Department of Basic Science, College of Dentistry, New York University, 345 E 24th Street, New York City, NY 10010, USA. Fax: +1 212 995 4087.

Department of Basic Science, College of Dentistry, New York University, New York, NY 10010, USA

Received 28 December 2009; received in revised form 16 June 2010; accepted 1 July 2010. published online 09 July 2010.

Abstract 

Protein–protein interactions between the Bcl2 family proteins regulate apoptosis. An imbalance of this interaction network due to the upregulation of the proto-oncogene Bcl2 leads to a resistance to apoptosis associated with tumor formation. Bcl2 overexpression inhibits BAX oligomerization and mitochondrial outer membrane (MOM) permeabilization. However, Bcl2 effects on earlier steps of BAX-mediated apoptosis are not fully understood. Bcl2 overexpression inhibits BAX insertion into the MOM but spontaneously increases BAX relocalization to the mitochondria. Also, a physical interaction between BAX and Bcl2 is necessary for these two effects to occur. Taken together, these results suggest upregulated Bcl2 stabilizes BAX loose binding to mitochondrial membranes, inhibiting its insertion into the MOM and consequently cytochrome c release.

Structured summary

MINT-7945271: BAX (uniprotkb:Q07813) physically interacts (MI:0915) with Bcl-2 (uniprotkb:P10417) by anti bait coimmunoprecipitation (MI:0006)

Keywords: Bcl2, BAX, Mitochondria, Apoptosis

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PII: S0014-5793(10)00556-9

doi:10.1016/j.febslet.2010.07.002

FEBS Letters
Volume 584, Issue 15 , Pages 3305-3310, 4 August 2010

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