| Type: | Family | Name: | Apoptosis regulator, Ced-4 |
| Description: | Apoptosis, or programmed cell death (PCD), is a common and evolutionarily conserved property of all metazoans []. In many biological processes, apoptosis is required to eliminate supernumerary or dangerous (such as pre-cancerous) cells and to promote normal development. Dysregulation of apoptosis can, therefore, contribute to the development of many major diseases including cancer, autoimmunity and neurodegenerative disorders. In most cases, proteins of the caspase family execute the genetic programme that leads to cell death.Ced-4 is a family of apoptosis proteins. Caenorhabditis eleganshas three genes, ced-3, ced-4 and ced-9, which code for the components of an induction pathway of apoptosis that is conserved in the nematode and mammals. Homologues in have also been found in Drosophila []. Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex. This allows ced-4 to activate the cell-killing caspase ced-3. Apoptotic protease-activating factor-1 (Apaf-1) is a key regulator of the mitochondrial apoptosis pathway. It consists of three functional regions: an N-terminal caspase recruitment domain (CARD) that can bind to procaspase-9, a CED-4-like region enabling self-oligomerization, and a regulatory C terminus with WD-40 repeats masking the CARD and CED-4 region [].DEFCAP a novel member of Ced-4 family of apoptosis proteins. It is similar to the other mammalian Ced-4 proteins (Apaf-1 and Nod1) in that it contains a caspase recruitment domain (CARD) and a putative nucleotide binding domain signified by a P-loop and magnesium binding site []. | Short Name: | Apop_reg_Ced-4 |
