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The Intrinsic Apoptotic Pathway01:31

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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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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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Strategies for Tracking Anastasis, A Cell Survival Phenomenon that Reverses Apoptosis
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Arrestins in apoptosis.

Seunghyi Kook1, Vsevolod V Gurevich, Eugenia V Gurevich

  • 1Department of Pharmacology, Vanderbilt University, 2200 Pierce Ave, Nashville, TN, 37232, USA.

Handbook of Experimental Pharmacology
|December 3, 2013
PubMed
Summary
This summary is machine-generated.

Arrestin-2 is cleaved by caspases during programmed cell death (apoptosis). This fragment aids in releasing cytochrome C, a key step in cell death, highlighting arrestin-2

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Programmed cell death (apoptosis) is a critical cellular process regulated by caspases.
  • Nonvisual arrestins influence cell death signaling pathways.
  • Previous studies show conflicting roles for arrestins in apoptosis.

Purpose of the Study:

  • To investigate the specific role of arrestin-2 in apoptosis.
  • To elucidate the mechanism by which arrestin-2 affects cell death.
  • To determine the evolutionary conservation of arrestin-2 cleavage in apoptosis.

Main Methods:

  • Analysis of caspase cleavage of arrestin-2.
  • Assessment of arrestin-2 fragment's role in cytochrome C release.
  • Comparison of wild-type and caspase-resistant arrestin-2 mutants in cell death assays.
  • Evolutionary analysis of the caspase cleavage site in arrestin-2.

Main Results:

  • Arrestin-2 is specifically cleaved by caspases during apoptosis.
  • The generated arrestin-2 fragment promotes cell death by assisting tBID in cytochrome C release from mitochondria.
  • The caspase cleavage site in arrestin-2 is conserved in vertebrates but not invertebrates.
  • A caspase-resistant arrestin-2 mutant failed to promote cell death.

Conclusions:

  • Arrestin-2 is a direct participant in the apoptotic cascade.
  • Cleavage of arrestin-2 by caspases is a conserved mechanism facilitating cell death.
  • Arrestin-2 cleavage represents a critical step in committing cells to apoptosis.