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Related Concept Videos

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.
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...
Cellular Injury V: Apoptosis and Autophagy01:22

Cellular Injury V: Apoptosis and Autophagy

Cells respond to damage and stress through highly coordinated processes that decide whether they survive or undergo controlled self-destruction. Two major pathways involved in this regulation are apoptosis, a type of programmed cell death, and autophagy, a survival mechanism that helps cells adapt to adverse conditions.ApoptosisApoptosis removes aged or injured cells to maintain tissue balance. During this process, the cell shrinks, chromatin condenses and fragments, and membrane-bound...
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...
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.

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Related Experiment Video

Updated: Jul 15, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

Bax activation and mitochondrial insertion during apoptosis.

Lisenn Lalier1, Pierre-François Cartron, Philippe Juin

  • 1INSERM U601, F-44000 Nantes, France.

Apoptosis : an International Journal on Programmed Cell Death
|April 25, 2007
PubMed
Summary

The mitochondrial apoptotic pathway, crucial for cell fate, is often disrupted in cancer. This review details how Bax protein activation by Bcl-2 family proteins initiates this pathway.

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Last Updated: Jul 15, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c
07:42

Activation of Apoptosis by Cytoplasmic Microinjection of Cytochrome c

Published on: June 29, 2011

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

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The mitochondrial apoptotic pathway regulates cell death and is frequently altered in cancer.
  • This pathway involves mitochondrial outer membrane (MOM) permeabilization, leading to apoptosis.
  • The Bcl-2 protein family controls MOM permeabilization, with both pro- and anti-apoptotic members.

Purpose of the Study:

  • This review focuses on the molecular mechanisms of Bax activation.
  • It specifically examines Bax interactions within the Bcl-2 protein family.
  • The review aims to elucidate Bax's role in initiating apoptosis.

Main Methods:

  • Literature review of molecular events in Bax activation.
  • Analysis of protein-protein interactions within the Bcl-2 family.
  • Focus on the regulation of Bax and Bak oligomerization.

Main Results:

  • Bcl-2 family proteins, including BH3-only proteins (BOPs) and anti-apoptotic proteins, antagonistically regulate Bax and Bak.
  • Bax activation is a critical step controlled by interactions with other Bcl-2 family members.
  • Oligomerization of Bax and Bak at the MOM triggers apoptotic mitochondrial permeabilization.

Conclusions:

  • Bax activation is a key event in the mitochondrial apoptotic pathway.
  • Understanding Bax regulation by the Bcl-2 family is crucial for cancer research.
  • Further studies will explore how activated Bax induces MOM permeabilization.