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The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

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Internal cellular stress, such as cellular injury or hypoxia, triggers intrinsic apoptosis. The B-cell lymphoma 2 (Bcl-2) family of proteins are the primary regulators of the intrinsic apoptotic pathway. For example, during DNA damage, checkpoint proteins, such as Ataxia Telangiectasia Mutated (ATM protein) and Checkpoints Factor-2 (Chk2) proteins, are activated. These proteins phosphorylate p53 which further activates pro-apoptotic proteins, such as Bax, Bak, PUMA, and Noxa, and inhibits...
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Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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The extrinsic apoptotic pathway is initiated when extracellular death-inducing signals, such as specific cytokines, activate the death receptors expressed on the cell surface. The immune cells involved in this pathway are natural killer cells (NK cells) and cytotoxic T-lymphocytes. NK cells are critical in innate immune response, while cytotoxic T-lymphocytes are associated with adaptive immune response. These cells recognize specific receptors expressed on the altered cells and activate...
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Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
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Structural basis of BAX pore formation.

Ying Zhang1, Lu Tian1, Gaoxingyu Huang2,3,4

  • 1Beijing Frontier Research Center for Biological Structure, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.

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Summary
This summary is machine-generated.

The protein BAX forms various ring-like structures to trigger apoptosis by permeabilizing mitochondrial membranes. Understanding BAX oligomer assembly reveals its mechanism in cell death.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Structural Biology

Background:

  • BAX protein is crucial for initiating apoptosis, the programmed cell death pathway.
  • Cytosolic BAX monomers translocate to mitochondria, permeabilizing the outer membrane to trigger cell death.

Purpose of the Study:

  • To elucidate the structural basis of BAX oligomerization and its role in mitochondrial outer membrane permeabilization.
  • To identify the fundamental repeating unit of BAX oligomers.

Main Methods:

  • Cryo-electron microscopy (Cryo-EM) at 3.2-angstrom resolution.
  • Structural characterization of BAX oligomeric forms (arcs, lines, rings).
  • Analysis of BAX protomer interactions and mutations.

Main Results:

  • A dimer of BAX dimers identified as the basic repeating unit.
  • Structural characterization of BAX repeating units and their assembly into higher-order oligomers (tetragon, pentagon, hexagon, heptagon).
  • Specific mutations at the BAX inter-protomer interface impair pore formation and proapoptotic function.

Conclusions:

  • The assembly principle of BAX oligomers provides a structural foundation for understanding BAX-mediated membrane permeabilization.
  • BAX oligomerization is a key mechanism controlling its proapoptotic activity.