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Details on Person Apoptotic protease-activating factor-1 (APAF1) is a multidom...
| Class:Id | Summation:6804577 |
|---|---|
| _displayName | Apoptotic protease-activating factor-1 (APAF1) is a multidom... |
| _timestamp | 2015-10-13 06:14:18 |
| created | [InstanceEdit:6804583] Shamovsky, Veronica, 2015-10-13 |
| literatureReference | [LiteratureReference:6804567] A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform [LiteratureReference:6804587] Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1 [LiteratureReference:6804597] Structure of an apoptosome-procaspase-9 CARD complex [LiteratureReference:6804598] The holo-apoptosome: activation of procaspase-9 and interactions with caspase-3 [LiteratureReference:1247977] The apoptosome: signalling platform of cell death [LiteratureReference:877384] NODs: intracellular proteins involved in inflammation and apoptosis [LiteratureReference:6804590] Wheel of Life, Wheel of Death: A Mechanistic Insight into Signaling by STAND Proteins [LiteratureReference:6804564] Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation [LiteratureReference:141214] Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. [LiteratureReference:6791361] Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis |
| text | Apoptotic protease-activating factor-1 (APAF1) is a multidomain adapter protein containing an N-terminal caspase recruitment domain (CARD), followed by a central nucleotide-binding/oligomerization domain (NOD, also known as NB-ARC) and a C-terminal regulatory region (Inohara N and Nunez G, 2003; Danot O et al., 2009; Yuan S et al. 2011). NOD can be subdivided into the nucleotide-binding (NBD), helical (HD1) and winged helix (WHD) domains. APAF1 is normally present as a monomer in an inactive, locked conformation bound to dATP or ATP (Kim HE et al., 2005). However, upon cytochrome c binding to its WDR, APAF1 is thought to undergo a conformational change, driven by ATP (or dATP) hydrolysis (Kim HE et al., 2005). The CARD and ancillary HD domains of APAF1 undergo additional conformational changes to expose its AAA+ ATPase domain and allow multiple APAF1 proteins to oligomerize into a circular heptameric apoptosome complex (Yu X et al. 2005; Riedl SJ and Salvesen GS, 2007; Yuan S et al., 2010, 2011). This process probably requires conformational changes coupled with nucleotide exchange (Kim HE et al., 2005; Yuan S et al., 2010). Cytochrome c is bound between the two beta-propellers and serves as the initial trigger for APAF1 assembly (Acehan D et al., 2002; Yu et al., 2005, Yuan S et al. 2010; Li P et al., 1997; Hu Y et al., 1999). |
| (summation) | [Reaction:6804579] APAF1:CYCS forms heptamer [Homo sapiens] |
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No pathways have been reviewed or authored by Apoptotic protease-activating factor-1 (APAF1) is a multidom... (6804577)
