Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drp1 and hFis1

Dejuan Kong, Liping Xu, Yingjie Yu, Weijia Zhu, David W. Andrews, Yisang Yoon, Tuan H. Kuo

Research output: Contribution to journalArticle

39 Scopus citations

Abstract

The regulation of mitochondrial permeability transition (MPT) is essential for cell survival. Un-controlled opening of the MPT pore is often associated with cell death. Anti-death protein Bcl-2 can block MPT as assessed by the enhanced capacity of mitochondria to accumulate and retain Ca2+. We report here that two proteins of the mitochondrial fission machinery, dynamin-related protein (Drp1) and human mitochondrial fission protein (hFis1), have an antagonistic effect on Bcl-2. Drp1, with the assistance of hFis1, sensitizes cells to MPT by reducing the mitochondrial Ca2+ retention capacity (CRC). While the reduction of CRC by Drp1/hFis1 is linked to mitochondrial fission, the antagonism between Bcl-2 and Drp1 appears to be mediated by mutually exclusive interactions of the two proteins with hFis1. The complexity of protein-protein interactions demonstrated in the present study suggests that in addition to the previously described role of Bcl-2 in the control of apoptosis, Bcl-2 may also participate directly or indirectly in the regulation of mitochondrial fission.

Original languageEnglish (US)
Pages (from-to)187-199
Number of pages13
JournalMolecular and Cellular Biochemistry
Volume272
Issue number1-2
DOIs
StatePublished - Apr 1 2005
Externally publishedYes

Keywords

  • Apotosis
  • Bcl-2
  • Calcium
  • Drp1
  • Mitochondria
  • Mitochondrial fission
  • Permeability transition
  • hFis1

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

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