Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid

Banerjee, Jyotirmoy; Ghosh, Subhendu

doi:10.1016/j.bbrc.2004.08.094

Cited by 77 publications

(48 citation statements)

References 28 publications

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“…In reconstitution studies in liposomes and phospholipid bilayers, Shimizu and coworkers (36) have reported that Bax can induce a novel highconductance state of VDAC that permits cytochrome c to escape from the intermembrane space. Similarly, a recent report demonstrated that Bax and tBid increased the conductance of VDAC in planar bilayers and enhanced cytochrome c translocation from the cis to the trans chamber (44). Interestingly, VDAC phosphorylation by PKA inhibited the effects of Bax and tBid (45).…”

Section: The Voltage-dependent Anion Channelmentioning

confidence: 67%

Mitochondrial Ion Channels

O’Rourke

2007

Annu. Rev. Physiol.

273

153

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In work spanning more than a century, mitochondria have been recognized for their multifunctional roles in metabolism, energy transduction, ion transport, inheritance, signaling, and cell death. Foremost among these tasks is the continuous production of ATP through oxidative phosphorylation, which requires a large electrochemical driving force for protons across the mitochondrial inner membrane. This process requires a membrane with relatively low permeability to ions to minimize energy dissipation. However, a wealth of evidence now indicates that both selective and nonselective ion channels are present in the mitochondrial inner membrane, along with several known channels on the outer membrane. Some of these channels are active under physiological conditions, and others may be activated under pathophysiological conditions to act as the major determinants of cell life and death. This review summarizes research on mitochondrial ion channels and efforts to identify their molecular correlates. Except in a few cases, our understanding of the structure of mitochondrial ion channels is limited, indicating the need for focused discovery in this area.

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Section: The Voltage-dependent Anion Channelmentioning

confidence: 67%

Mitochondrial Ion Channels

O’Rourke

2007

Annu. Rev. Physiol.

273

153

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“…As Bax and Bak can also form pores, this leads to the intriguing situation of interaction between two different pore-forming proteins. Bax binding may enlarge VDAC pores to a size compatible with cytochrome c passage (Banerjee and Ghosh, 2004); additionally, VDAC-only pores for cytochrome c release may form . A model of VDAC organization is shown in Fig.…”

Section: Cooperation With Vdac/porinmentioning

confidence: 99%

Multistep and multitask Bax activation

Ghibelli

Diederich

2010

Mitochondrion

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Bax is a pro-apoptotic protein allowing apoptosis to occur through the intrinsic, damage-induced pathway, and amplifying that one occurring via the extrinsic, receptor mediated pathway. Bax is present in viable cells and activated by pro-apoptotic stimuli. Activation implies structural changes, consisting of exposure of the N terminus and hydrophobic domains; changes in localization, consisting in migration from cytosol to mitochondria and endoplasmic reticulum membranes; changes in the aggregation status, from monomer to dimer and multimer. Bax has multiple critical domains, namely the N terminus exposed after activation; two hydrophobic stretches exposed for membrane anchorage; two reactive cysteines allowing multimerization; the BH3 domain for interactions with the Bcl-2 family members; alpha helix 1 for t-Bid interaction. Bax has also multiple functions: it releases different mitochondrial factors such as cytochrome c, SMAC/diablo; it regulates mitochondrial fission, the mitochondrial permeability transition pore; it promotes Ca 2+ leakage through ER membrane. Altogether, Bax activation is a complex multi-step phenomenon. Here, we analyze these events as logically separable or alternative steps, attempting to assess their role, timing and reciprocal relation.

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“…(2) Pro-apoptotic factors may act directly on the lipidic component of the OM, or at the lipidprotein interface, thus favoring the formation of pores though which IMS proteins may exit to the cytosol [29,[44][45][46]. (3) Activated pro-apoptotic members of the Bcl-2 family may interact with components of the permeability transition pore complex (PTPC), thus favoring (or de-inhibiting) the permeability transition (PT) of the IM, that in turn leads to the physical rupture of the OM [47][48][49]. In this latter case, IM would supply an active contribution to MMP, as we will briefly discuss in the next section.…”

Section: Om Permeabilizationmentioning

confidence: 99%

Methods for the assessment of mitochondrial membrane permeabilization in apoptosis

et al. 2007

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Mitochondrial membrane permeabilization (MMP) is considered as the "point-of-no-return" in numerous models of programmed cell death. Indeed, mitochondria determine the intrinsic pathway of apoptosis, and play a major role in the extrinsic route as well. MMP affects the inner and outer mitochondrial membranes (IM and OM, respectively) to a variable degree. OM permeabilization culminates in the release of proteins that normally are confined in the mitochondrial intermembrane space (IMS), including caspase activators (e.g. cytochrome c) and caspase-independent death effectors (e.g. apoptosis-inducing factor). Partial IM permeabilization disrupts mitochondrial ion and volume homeostasis and dissipates the mitochondrial transmembrane potential ( m ). The assessment of early mitochondrial alterations allows for the identification of cells that are committed to die but have not displayed yet the apoptotic phenotype. Several

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Bax increases the pore size of rat brain mitochondrial voltage-dependent anion channel in the presence of tBid

Cited by 77 publications

References 28 publications

Mitochondrial Ion Channels

Mitochondrial Ion Channels

Multistep and multitask Bax activation

Methods for the assessment of mitochondrial membrane permeabilization in apoptosis

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