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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...
Overview of Cell Death01:30

Overview of Cell Death

Cell death is an essential process where the body gets rid of old or damaged cells. Cell proliferation and death need to be balanced, as an imbalance between the two may lead to cancer or autoimmune diseases.
Cell death was observed in the early 19th century, but there was no experimental evidence to prove it. In 1842, Carl Vogt first discovered cell death in a metamorphic toad; however, it was not termed ‘cell death.’ Scientists discovered different cell death pathways only in the 20th century...
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.
Autophagic Cell Death01:18

Autophagic Cell Death

Christian de Duve discovered “autophagy,” a process in which cellular components are engulfed by membrane-bound organelles called autophagosomes. The autophagosomes then fuse with lysosomes to digest the enclosed contents. Autophagy is generally activated in cells to prevent cell death. However, cell death is triggered when the damage is beyond repair.
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and pro-apoptotic...

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Related Experiment Video

Updated: May 18, 2026

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

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation

Published on: March 5, 2018

Death by caspase dimerization.

Sarah H MacKenzie1, A Clay Clark

  • 1Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina, USA.

Advances in Experimental Medicine and Biology
|September 6, 2012
PubMed
Summary
This summary is machine-generated.

Caspases, key proteins in apoptosis (controlled cell death), require dimerization for activation. This process is crucial for forming functional proteases essential for cell dismantling.

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Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex
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Last Updated: May 18, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
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Measuring Composition of CD95 Death-Inducing Signaling Complex and Processing of Procaspase-8 in this Complex

Published on: August 2, 2021

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Controlled cell death, or apoptosis, is a fundamental biological process involving a cascade of molecular events.
  • Caspases, a family of proteases, are central executioners of the apoptotic pathway.
  • Caspases are classified as initiator or effector proteases based on their role in the apoptosis cascade.

Purpose of the Study:

  • To elucidate the critical role of dimerization in the activation and function of caspases.
  • To understand how dimerization contributes to the specific activation mechanisms of initiator and effector caspases.
  • To highlight the importance of the dimer interface in caspase stability and active site formation.

Main Methods:

  • Analysis of caspase activation mechanisms, focusing on the transition from monomers or zymogens to active forms.
  • Investigation of the structural and biochemical properties of caspase dimers.
  • Examination of the dimer interface interactions and their contribution to protease function.

Main Results:

  • Initiator caspases require dimerization for activation, while effector caspases need processing of dimeric zymogens.
  • Dimerization is essential for the formation of a fully functional caspase active site, with contributions from both monomers.
  • Unique interactions within the dimer interface dictate the stability and specific activation modes of different caspases.

Conclusions:

  • Dimerization is a pivotal regulatory step in caspase activation, essential for initiating and executing apoptosis.
  • The structural integrity of caspase dimers, particularly the dimer interface, is critical for their proteolytic activity.
  • Understanding caspase dimerization provides insights into the precise control of programmed cell death.