Related Experiment Video
Updated: Aug 1, 2026

13:21
In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila
Published on: November 27, 2016
Caspases rule the intracellular trafficking cartel
Catherine Duclos1, Christine Lavoie1, Jean-Bernard Denault1
1Institut de Pharmacologie de Sherbrooke, Department of Pharmacology-Physiology, Faculty of Medicine and Health Sciences, Université de Sherbrooke, QC, Canada.
The FEBS Journal
|April 4, 2017
Summary
During programmed cell death (apoptosis), caspases dismantle cellular proteins, including those vital for intracellular trafficking. This review explores how caspases disrupt the cell
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Apoptosis is a critical cellular process involving caspases, a family of proteases.
- Caspases execute cellular demise by cleaving numerous cellular proteins.
- Intracellular trafficking is essential for cellular function and communication.
Purpose of the Study:
- To review the mechanisms by which caspases target proteins involved in intracellular trafficking.
- To elucidate the consequences of caspase-mediated disruption of the trafficking machinery.
- To highlight the role of caspases in cellular dismantling through the lens of transport processes.
Main Methods:
- Literature review of studies on caspases and intracellular trafficking.
- Analysis of known caspase substrates and their roles in transport.
- Synthesis of findings on the impact of caspase activity on vesicular transport and protein localization.
Main Results:
- Caspases proteolyze key proteins regulating vesicle formation, movement, and fusion.
- Disruption of intracellular trafficking by caspases leads to cellular dysfunction and contributes to apoptotic morphology.
- Specific examples of targeted trafficking proteins and their functional impairment are discussed.
Conclusions:
- Caspase-mediated cleavage of trafficking proteins is a significant aspect of apoptosis.
- Targeting the transport machinery is a crucial strategy employed by caspases to ensure efficient cellular dismantling.
- Understanding these interactions provides insights into cell death pathways and potential therapeutic targets.
Related Concept Videos
Regulated Protein Degradation
It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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.
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 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 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...
Phagocytosis of Apoptotic Cells
Cells undergoing apoptosis form apoptotic bodies that must be removed immediately to prevent inflammation, autoimmune diseases, and necrosis. Phagocytosis is carried out by professional phagocytes such as macrophages or immature dendritic cells. Non-professional phagocytes such as epithelial cells and fibroblasts also take part in this process; however, they are not as effective as professional phagocytes.
Normal cells contain receptors that prevent them from being recognized by phagocytes.
Normal cells contain receptors that prevent them from being recognized by phagocytes.

