Related Experiment Video

Updated: Jun 21, 2025

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

7.9K

The C-terminal sequences of Bcl-2 family proteins mediate interactions that regulate cell death

Dang Nguyen1,2, Elizabeth Osterlund3, Justin Kale2

  • 1Department of Medical Biophysics, Faculty of Medicine, University of Toronto, Toronto, Canada.

The Biochemical Journal
|July 10, 2024
PubMed

Insights

Conserved C-terminal sequences (CTSs) regulate programmed cell death by mediating Bcl-2 family protein interactions. These interactions control apoptosis via mitochondrial outer membrane permeabilization (MOMP).

Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Programmed cell death, or apoptosis, is crucial for multicellular organisms.
  • The Bcl-2 protein family regulates apoptosis by controlling mitochondrial outer membrane permeabilization (MOMP).

Purpose of the Study:

  • To review the critical role of conserved C-terminal sequences (CTSs) in Bcl-2 family protein interactions.
  • To elucidate how CTSs mediate protein-protein binding and influence MOMP regulation.

Main Methods:

  • Literature review of studies on Bcl-2 family proteins and their interactions.
  • Analysis of the structural and functional significance of CTSs in apoptosis regulation.

Main Results:

  • CTSs mediate crucial homotypic and heterotypic interactions within the Bcl-2 protein family.
  • These interactions dictate the commitment to apoptosis through MOMP.
  • CTSs are involved in interactions that promote or inhibit MOMP.

Conclusions:

  • CTSs are key regulators of Bcl-2 family protein interactions.
  • Understanding CTS function is vital for comprehending apoptosis control.
  • CTSs represent potential targets for therapeutic interventions in diseases involving apoptosis dysregulation.
Keywords:
BH3-only proteinsBaxBcl-2apoptosisprotein–protein interactionstransmembrane domain

More Related Videos

Identifying Protein-protein Interaction Sites Using Peptide Arrays07:44

Identifying Protein-protein Interaction Sites Using Peptide Arrays

Published on: November 18, 2014

18.0K
Applying an Inducible Expression System to Study Interference of Bacterial Virulence Factors with Intracellular Signaling08:51

Applying an Inducible Expression System to Study Interference of Bacterial Virulence Factors with Intracellular Signaling

Published on: June 25, 2015

9.2K

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...
6.5K
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...
6.3K
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...
12.4K
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...
11.3K
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...
7.2K
Canonical Wnt Signaling Pathway02:54

Canonical Wnt Signaling Pathway

The gene encoding the main signaling molecules of the Wnt signaling pathways (the Wnt proteins) was discovered almost four decades ago by Nüsslein-Volhard and Wieschaus. They identified and originally named the gene "wingless" (wg) after a phenotype discovered during their landmark genetic screen in Drosophila for body pattern defects. At around the same time, another researcher named Harold Varmus found that a murine tumor virus activates the mammalian wg homolog, Int-1, which...
8.7K