Membrane Remodeling Induced by the Dynamin-Related Protein Drp1 Stimulates Bax Oligomerization
Sylvie Montessuit,Syam Prakash Somasekharan,Oihana Terrones,Safa Lucken-Ardjomande,Sébastien Herzig,Robert Schwarzenbacher,Dietmar J. Manstein,Ella Bossy-Wetzel,Gorka Basañez,Paolo Meda,Jean-Claude Martinou +10 more
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TLDR
It is shown that Drp1 stimulates tBid-induced Bax oligomerization and cytochrome c release by promoting tethering and hemifusion of membranes in vitro by exploiting arginine 247 and the presence of cardiolipin in membranes.Citations
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Mitochondrial Fission, Fusion, and Stress
TL;DR: In their Perspective, Hoppins and Nunnari explain that the endoplasmic reticulum is an active participant in mitochondrial division and discuss how mitochondrial dynamics and cell death are linked.
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Mitochondria: In Sickness and in Health
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Mitochondrial form and function
TL;DR: Recent advances have revealed how the organelle's behaviour has evolved to allow the accurate transmission of its genome and to become responsive to the needs of the cell and its own dysfunction.
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Mitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics
TL;DR: Fission of mitochondria has been reported to participate in apoptosis in Drosophila and Caenorhabditis elegans, however, in these organisms, mitochondrial membrane permeabilization does not occur and the mechanism by which mitochondrial dynamics participates in cell death remains elusive.
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Mitochondrial dynamics in the regulation of nutrient utilization and energy expenditure.
TL;DR: Placement of bioenergetic adaptation and quality control as competing tasks of mitochondrial dynamics might provide a new mechanism, linking excess nutrient environment to progressive mitochondrial dysfunction, common to age-related diseases.
References
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The BCL-2 protein family: opposing activities that mediate cell death
TL;DR: New insights into interactions among BCL-2 family proteins reveal how these proteins are regulated, but a unifying hypothesis for the mechanisms they use to activate caspases remains elusive.
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Mitochondrial Membrane Permeabilization in Cell Death
TL;DR: Once MMP has been induced, it causes the release of catabolic hydrolases and activators of such enzymes (including those of caspases) from mitochondria, meaning that mitochondria coordinate the late stage of cellular demise.
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The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis.
Stephan Frank,Brigitte Gaume,Elke S. Bergmann-Leitner,Wolfgang W. Leitner,Everett G. Robert,Frédéric Catez,Carolyn L. Smith,Richard J. Youle +7 more
TL;DR: In healthy cells, fusion and fission events participate in regulating mitochondrial morphology and inhibition of Drp1 blocks cell death, implicating mitochondrial fission as an important step in apoptosis.
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Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane.
Tomomi Kuwana,Mason R. Mackey,Guy Perkins,Mark H. Ellisman,Martin Latterich,Roger Schneiter,Douglas R. Green,Donald D. Newmeyer +7 more
TL;DR: It is concluded that mitochondrial protein release in apoptosis can be mediated by supramolecular openings in the outer mitochondrial membrane, promoted by BH3/Bax/lipid interaction and directly inhibited by Bcl-x(L).
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Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis
Solange Desagher,Astrid Osen-Sand,Anthony Nichols,Robert Eskes,Sylvie Montessuit,Sandra Lauper,Kinsey Maundrell,Bruno Antonsson,Jean-Claude Martinou +8 more
TL;DR: The results suggest that, during certain types of apoptosis, Bid translocates to mitochondria and binds to Bax, leading to a change in conformation of Bax and to cytochrome c release from mitochondria.