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Updated: May 5, 2026

Lighting Up the Pathways to Caspase Activation Using Bimolecular Fluorescence Complementation
Published on: March 5, 2018
Caspase cleavage is not for everyone
Carrie E Johnson1, Sally Kornbluth
1Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27710, USA.
Abstract:
During apoptosis, caspases cleave cellular substrates to break down and package the apoptotic cell for removal. Reporting in Cell, Mahrus et al. (2008) and Dix et al. (2008) use new approaches that identify hundreds of previously unrecognized caspase substrates, many of which appear to produce polypeptide fragments with potentially new functional activities.
Insights
New research identifies hundreds of previously unknown caspase substrates during apoptosis. These substrates generate polypeptide fragments with potential novel functions, advancing our understanding of programmed cell death.
Area of Science:
- Cellular biology
- Molecular biology
- Biochemistry
Background:
- Apoptosis, or programmed cell death, involves caspases cleaving cellular substrates.
- This cleavage facilitates the breakdown and packaging of the cell for removal.
Discussion:
- Mahrus et al. (2008) and Dix et al. (2008) employed novel methodologies to identify caspase substrates.
- These studies uncovered hundreds of previously unrecognized targets of caspase activity.
Key Insights:
- A significant number of newly identified caspase substrates yield polypeptide fragments.
- These fragments may possess previously undiscovered functional roles within the cell.
Outlook:
- Further investigation into the functions of these novel polypeptide fragments is warranted.
- This research opens new avenues for understanding the complex mechanisms of apoptosis and cellular signaling.
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