Regulation of Ca2+-induced permeability transition by Bcl-2 is antagonized by Drpl and hFis1 - PubMed (original) (raw)

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

Dejuan Kong et al. Mol Cell Biochem. 2005 Apr.

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.

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References

    1. J Biol Chem. 2001 Jan 26;276(4):2571-5 - PubMed
    1. Cell. 2002 Nov 1;111(3):331-42 - PubMed
    1. Nat Rev Mol Cell Biol. 2003 Jul;4(7):552-65 - PubMed
    1. Anal Biochem. 1984 Mar;137(2):360-7 - PubMed
    1. J Cell Sci. 2004 Mar 1;117(Pt 7):1201-10 - PubMed

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