Cytochrome c Release upon Fas Receptor Activation Depends on Translocation of Full-length Bid and the Induction of the Mitochondrial Permeability Transition

Tafani, Marco; Karpinich, Natalie O.; Hurster, Kathryn A.; Pastorino, John G.; Schneider, Timothy; Russo, Matteo Antonio; Farber, John L.

doi:10.1074/jbc.m111350200

Cited by 117 publications

(102 citation statements)

References 51 publications

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“…A recent report (32) suggests that the insertion of Bax in the outer membrane may result in the de novo formation of contact sites. These and other (33)(34)(35)(36)(37) findings suggest that Bax (and perhaps its homologues Bak and Bid) may induce the mitochondrial PT and cytochrome c release by interacting with the PTP to either form or regulate it (or both). Anti-apoptotic Bcl-2 family members antagonize the permeability transition (38) and inhibit activity by reconstituted PTPC (23,39), but this antagonistic action takes place regardless of the presence of Bax in the complex (23).…”

mentioning

confidence: 76%

Bax Does Not Directly Participate in the Ca2+-induced Permeability Transition of Isolated Mitochondria

Marchi¹,

Campello²,

Szabó

et al. 2004

Journal of Biological Chemistry

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The mitochondrial permeability transition pore and Bax have both been proposed to be involved in the release of pro-apoptotic factors from mitochondria in the "intrinsic" pathway of apoptosis. The permeability transition pore is widely thought to be a supramolecular complex including or interacting with Bax. Given the relevance of the permeability transition in vivo, we have verified whether Bax influences the formation and/or the properties of the Ca 2؉ /P i -induced permeability transition by using mitochondria isolated from isogenic human colon cancer bax ؉/؊ and bax ؊/؊ HCT116 cell lines. We used mitochondria isolated from both types of cells and from Bax ؉ cells exposed to apoptotic stimuli, as well as Bax-less mitochondria into which exogenous Bax had been incorporated. All exhibited the same behavior and pharmacological profile in swelling and Ca 2؉ -retention experiments. Mitochondria from a bax ؊ /bak ؊ cell line also underwent an analogous Ca 2؉ /P i -inducible swelling. This similarity indicates that Bax has no major role in regulating the Ca 2؉ -induced mitochondrial permeability transition.

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mentioning

confidence: 76%

Bax Does Not Directly Participate in the Ca2+-induced Permeability Transition of Isolated Mitochondria

Marchi¹,

Campello²,

Szabó

et al. 2004

Journal of Biological Chemistry

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“…It is possible that the localized activity of caspase-8 helps ensure that the cleavage of Bid is performed where it is functionally needed: on the surface of the mitochondria. Although Bid was first described as a cytosolic protein (Wang et al, 1996;Li et al, 1998;Luo et al, 1998), several laboratories have reported its detection at the surface of mitochondria (Esposti et al, 2001;Grinberg et al, 2002;Tafani et al, 2002). Moreover, CL promotes tBid binding to the mitochondrial outer membrane (Lutter et al, 2000;Gonzalvez et al, 2005a, b).…”

Section: Recent Advances In Understanding Apoptosis Initiationmentioning

confidence: 99%

New insights into apoptosis signaling by Apo2L/TRAIL

2010

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“…56 Full-length BID is also capable of translocation to the mitochondria in at least one case facilitated by other proteins such as PACS2. [57][58][59] At the mitochondria, full-length BID has been shown to potentiate cell death following certain apoptotic signals, suggesting that caspase cleavage is not an absolute requirement for activating BID's proapoptotic function. 58,60 Recent studies indicate that activation of BID's prodeath activity may be negatively regulated by phosphorylation.…”

Section: Proapoptotic Bidmentioning

confidence: 99%

BCL2 family in DNA damage and cell cycle control

2006

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Individual BCL2 family members couple apoptosis regulation and cell cycle control in unique ways. Antiapoptotic BCL2 and BCL-x L are antiproliferative by facilitating G0. BAX is proapoptotic and accelerates S-phase progression. The dual functions in apoptosis and cell cycle are coordinately regulated by the multi-domain BCL2 family members (MCL-1) and suggest that survival is maintained at the expense of proliferation. The role of BH3-only molecules in cell cycle is more variable. BAD antagonizes both the cell cycle and antiapoptotic functions of BCL2 and BCL-x L through BH3 binding. BID has biochemically separable functions in apoptosis and S-phase checkpoint, determined by posttranslational modification. p53-induced PUMA is known only to have apoptotic function. Inhibition of apoptosis is oncogenic, whereas promotion of cell cycle arrest is tumor suppressive. Paradoxically, selected BCL2 family members can be both oncogenic and tumor suppressive. Which of the dual functions predominates is lineage specific and context dependent.

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Cytochrome c Release upon Fas Receptor Activation Depends on Translocation of Full-length Bid and the Induction of the Mitochondrial Permeability Transition

Cited by 117 publications

References 51 publications

Bax Does Not Directly Participate in the Ca2+-induced Permeability Transition of Isolated Mitochondria

Bax Does Not Directly Participate in the Ca2+-induced Permeability Transition of Isolated Mitochondria

New insights into apoptosis signaling by Apo2L/TRAIL

BCL2 family in DNA damage and cell cycle control

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