Journal
MOLECULAR AND CELLULAR BIOCHEMISTRY
Volume 272, Issue 1-2, Pages 187-199Publisher
SPRINGER
DOI: 10.1007/s11010-005-7323-3
Keywords
mitochondria; permeability transition; Bcl-2; Drp1; hFis1; mitochondrial fission; apotosis; calcium
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Funding
- NHLBI NIH HHS [HL 39481] Funding Source: Medline
- NIDDK NIH HHS [DK61991] Funding Source: Medline
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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.
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