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Related Concept Videos

Caspases01:24

Caspases

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 cells.
The Extrinsic Apoptotic Pathway01:17

The Extrinsic Apoptotic Pathway

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...
The Intrinsic Apoptotic Pathway01:31

The Intrinsic Apoptotic Pathway

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...
Apoptosis01:30

Apoptosis

Apoptosis is a combination of two Greek words, 'apo' and 'ptosis,' meaning separation and falling off, respectively. Hippocrates used this word to describe gangrene, which was caused due to bandaging of fractured bones. Apoptosis was distinguished from necrosis in 1970 when John Kerr reported observations of morphological changes occurring during apoptosis. During one experiment, he observed that the disruption of blood supply to the liver tissue resulted in a size reduction of the tissue.
CRISPR and crRNAs02:53

CRISPR and crRNAs

Bacteria and archaea are susceptible to viral infections just like eukaryotes; therefore, they have developed a unique adaptive immune system to protect themselves. Clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins (CRISPR-Cas) are present in more than 45% of known bacteria and 90% of known archaea.
The CRISPR-Cas system stores a copy of foreign DNA in the host genome and uses it to identify the foreign DNA upon reinfection. CRISPR-Cas has three different...
DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...

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Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
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Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches

Published on: October 13, 2022

The unpredictable caspase-2: what can it do?

Helin Vakifahmetoglu-Norberg1, Boris Zhivotovsky

  • 1Division of Toxicology, Institute of Environmental Medicine, Karolinska Institutet, SE-171 77 Stockholm, Sweden.

Trends in Cell Biology
|January 12, 2010
PubMed
Summary
This summary is machine-generated.

Caspase-2, a key apoptosis regulator, has newly discovered roles in cell cycle and DNA repair, potentially acting as a tumor suppressor. PIDDosome complexes may control these diverse caspase-2 functions.

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Last Updated: Jun 17, 2026

Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
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Published on: October 13, 2022

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
08:47

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Published on: March 5, 2018

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry
05:29

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Published on: March 24, 2023

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Caspase-2 is a highly conserved caspase family protein crucial for apoptosis regulation.
  • Its exact function has been debated due to a lack of clear phenotypes in knockout mice.
  • Recent studies highlight novel activation mechanisms and roles beyond apoptosis.

Purpose of the Study:

  • To explore the multifaceted roles of caspase-2.
  • To discuss the involvement of PIDDosome complexes in regulating caspase-2 functions.
  • To connect caspase-2 activity to p53 and non-apoptotic processes.

Main Methods:

  • Review of recent publications on caspase-2 activation and function.
  • Analysis of the role of the PIDDosome complex.
  • Integration of evidence for caspase-2 in apoptosis, cell cycle, and DNA repair.

Main Results:

  • Caspase-2 activation is regulated by complexes like the PIDDosome.
  • Caspase-2 links to p53, suggesting roles in DNA damage response.
  • Evidence supports caspase-2 involvement in cell cycle regulation and DNA repair.
  • A tumor-suppressor role for caspase-2 is increasingly suggested.

Conclusions:

  • PIDDosome complexes are central to switching between caspase-2's diverse functions.
  • Caspase-2 plays critical roles in both apoptotic and non-apoptotic cellular processes.
  • Understanding these mechanisms is key to elucidating caspase-2's tumor-suppressor potential.