Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 9027312.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
Abstract
Previous genetic studies of the nematode Caenorhabditis elegans identified three important components of the cell death machinery. CED-3 and CED-4 function to kill cells, whereas CED-9 protects cells from death. Here CED-9 and its mammalian homolog Bcl-xL (a member of the Bcl-2 family of cell death regulators) were both found to interact with and inhibit the function of CED-4. In addition, analysis revealed that CED-4 can simultaneously interact with CED-3 and its mammalian counterparts interleukin-1beta-converting enzyme (ICE) and FLICE. Thus, CED-4 plays a central role in the cell death pathway, biochemically linking CED-9 and the Bcl-2 family to CED-3 and the ICE family of pro-apoptotic cysteine proteases.
Medical subject headings
- Apoptosis
- Caenorhabditis elegans
- Caenorhabditis elegans Proteins
- Calcium-Binding Proteins
- Caspases
- Cysteine Endopeptidases
- Helminth Proteins
- Proto-Oncogene Proteins
- Proto-Oncogene Proteins c-bcl-2