Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane.

By T. Kuwana, Mason R. Mackey, G. Perkins, Mark Ellisman, M. Latterich, R. Schneiter, Douglas R. Green, D. Newmeyer. Cell, 2002

1,544 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/96c616a82ac4ec5c04a69b2fe0765e38e2ba8f81

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Citations in the corpus

Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members. (2006, background): “Our results consistently show that ligation of antiapoptotic family members alone is insufficient to induce MOMP.”
The Bcl-2 family: roles in cell survival and oncogenesis (2003, background): “Both Bid and the lipid composition of the membrane appear to be important in facilitating Bax-induced porosity, although the nature of the pores remains in dispute (Kuwana et al., 2002; Roucou et al., 2002).”
The Bcl-2 apoptotic switch in cancer development and therapy (2007, background): “…activation can occur in some circumstances, to account for the ability of tBid or a Bid BH3 peptide with a chemically stabilized a-helix or one targeted to membranes to cooperate with Bax in the lysis of protein-free liposomes (Kuwana et al., 2002, 2005; Oh et al., 2006; Walensky et al., 2006).”
Elimination of Mcl-1 is required for the initiation of apoptosis following ultraviolet irradiation. (2003, background): “These complexes may function as protein pores for cytochrome c and other proteins to pass through, or cause mitochondrial outer membrane destabilization (Vander Heiden et al. 1997; Kuwana et al. 2002).”
Mitochondria and Mitophagy: The Yin and Yang of Cell Death Control (2012, background): “Upon activation, BAX and BAK form pores in the outer mitochondrial membrane large enough to allow for the passage of cytotoxic proteins from the intermembrane space to the cytosol (Figure 2A).(17) The regulation of apoptosis in the heart by BCL-2 proteins has been implicated in the pathogenesis of c”
JNK Signaling in Apoptosis (2008, background): “The activated Bax forms membrane channels through which apoptogenic proteins such as cytochrome c can be released (Bossy-Wetzel and Green, 1999; Kuwana et al., 2002; Madesh et al., 2002).”
Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax. (2008, background): “…interactions between BH3-only proteins and Bax (Willis et al., 2007), whereas in other studies, membrane permeabilization in cells, isolated mitochondria, or liposomes by full-length Bax usually depends upon addition of either a BH3 protein or peptide (Kuwana et al., 2002; Billen et al., 2008).”
Toxic proteins released from mitochondria in cell death (2004, background): “In most apoptotic conditions, the OMM becomes permeable, resulting in the leakage of cytochrome c into the cytosol by a process controlled by Bcl2 family members (Kluck et al., 1997; Yang et al., 1997; Cory and Adams, 2002).”
Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins. (2005, background): “Alternatively, Bax may be activated via direct engagement by certain BH3-only proteins, the best documented being the active truncated form of Bid, tBid (Wei et al. 2000; Kuwana et al. 2002; Roucou et al. 2002).”