Bid Induces the Oligomerization and Insertion of Bax into the Outer Mitochondrial Membrane

By Robert Eskes, S. Desagher, B. Antonsson, J. Martinou. Molecular and Cellular Biology, 2000

1,237 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/8e8cda4ebb2a55f5bb2ba8658519638d8180ece2

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Citations in the corpus

Breaking the mitochondrial barrier (2001, background): “Although we and others failed to detect any interaction between components of the PTP and Ba”
Mitochondria in Apoptosis: Bcl-2 family Members and Mitochondrial Dynamics (2011, background): “…Role of BH3-Only Proteins and of the Lipid Bilayer The protein tBid has been originally described as a direct activator of Bax, able to induce a conformational change of the Bax N terminus, as well as modulate Bax insertion and oligomerization in the OMM (Desagher et al., 1999; Eskes et al., 2000).”
The combined functions of proapoptotic Bcl-2 family members bak and bax are essential for normal development of multiple tissues. (2000, background): “…Author M anuscript N IH -PA Author M anuscript Bax and Bak have also been proposed as important mediators of the cell-extrinsic death pathway, acting as molecules that interact with the caspase substrate, Bid, to induce cytochrome c release from mitochondria (Eskes et al., 2000; Wei et al., 2000).”
BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. (2001, background): “…(Green and Reed, 1998). resulting in an allosteric conformational activation of The BCL-2 family of proteins is a critical death regulator BAK and BAX, including their intramembranous oligothat resides immediately upstream of the mitochondria merization (Eskes et al., 2000; Wei et al., 2000).”
Bcl-2 family proteins and cancer (2008, background): “Induction of MOMP correlates with oligomerization of Bax and/or Bak in the outer mitochondrial membrane, which is opposed by antiapoptotic proteins such as Bcl-2 and Bcl-XL (Eskes et al., 2000; Wei et al., 2000; Chipuk and Green, 2008).”
Role of Bcl-2 family proteins and caspases in the regulation of apoptosis (2011, background): “It is now well established that tBid leads to oligomerization of Bax and Bak, which forms pores in OMM which in turn permits the release of IMS proteins into the cytosol [54, 69].”
Bcl-2 family members: intracellular targeting, membrane-insertion, and changes in subcellular localization (2004, background): “In the case of the multidomain Bcl-2 family members Bax and Bcl-w, their TMDs are folded back into a hydrophobic pocket formed by the protein [40,50,51].”
Caspase-9, caspase-3 and caspase-7 have distinct roles during intrinsic apoptosis (2013, background): “Activation of the BCL-2 family members Bax and Bak results in MOMP and the release of pro-apoptotic proteins, including cytochrome c, from the inter-membrane space into the cytosol [3-5].”
Apoptotic pathways: paper wraps stone blunts scissors. (2000, background): “The interaction causes the latter to oligoship, and with it the power to kill the new cell through merize and insert into the mitochondrial membrane the production of reactive oxygen species, a mechanism (Eskes et al., 2000).”
c-MYC: more than just a matter of life and death (2002, background): “During apoptosis, BAX (normally an inactive monomer) can be induced to oligomerize and migrate from the cytoplasm to the mitochondria by various BH3-ONLY PROTEINS”