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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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: May 22, 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

Structural features of caspase-activating complexes.

Hyun Ho Park1

  • 1Department of Biochemistry, School of Biotechnology at Yeungnam University, Gyeongsan 712-749, Korea.

International Journal of Molecular Sciences
|May 19, 2012
PubMed
Summary
This summary is machine-generated.

Programmed cell death (apoptosis) is vital for multicellular life. This review details the structure and assembly of caspase-activating complexes, crucial for controlling apoptosis and preventing diseases like cancer.

Keywords:
DISCPIDDosomeapoptosisapoptosomecaspaseinflammationprotein structure

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Last Updated: May 22, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
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Published on: March 5, 2018

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

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

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Published on: March 24, 2023

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Apoptosis, or programmed cell death, is essential for organism development and homeostasis.
  • Dysregulation of apoptosis is linked to diseases such as cancer and neurodegeneration.
  • Caspase activation, mediated by specific protein complexes, drives the apoptotic process.

Purpose of the Study:

  • To review structural and biochemical studies of caspase-activating complexes.
  • To elucidate the molecular mechanisms underlying the assembly of these complexes.
  • To provide a comprehensive understanding of caspase activation.

Main Methods:

  • Literature review of structural and biochemical studies.
  • Analysis of existing data on caspase-activating complex assembly.
  • Comparative analysis of DISC, Apoptosome, and PIDDosome structures and functions.

Main Results:

  • Caspase-activating complexes (DISC, Apoptosome, PIDDosome) recruit and activate initiator caspases.
  • Structural and biochemical data reveal the assembly mechanisms of these complexes.
  • Understanding these mechanisms is key to comprehending caspase activation pathways.

Conclusions:

  • Caspase-activating complexes are critical oligomeric platforms for initiating apoptosis.
  • Structural insights into complex assembly provide a basis for understanding caspase regulation.
  • Further research into these complexes can inform therapeutic strategies for apoptosis-related diseases.