APAF1

APAF1

Apoptotic peptidase activating factor 1, also known as APAF1, is a human gene.

PBB_Summary
section_title =
summary_text = This gene encodes a cytoplasmic protein that initiates apoptosis. This protein contains several copies of the WD-40 domain, a caspase recruitment domain (CARD), and an ATPase domain (NB-ARC). Upon binding cytochrome c and dATP, this protein forms an oligomeric apoptosome. The apoptosome binds and cleaves caspase 9 preproprotein, releasing its mature, activated form. Activated caspase 9 stimulates the subsequent caspase cascade that commits the cell to apoptosis. Alternative splicing results in several transcript variants encoding different isoforms.cite web | title = Entrez Gene: APAF1 apoptotic peptidase activating factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=317| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Smith TF, Gaitatzes C, Saxena K, Neer EJ |title=The WD repeat: a common architecture for diverse functions. |journal=Trends Biochem. Sci. |volume=24 |issue= 5 |pages= 181–5 |year= 1999 |pmid= 10322433 |doi=10.1016/S0968-0004(99)01384-5
*cite journal | author=van Oirschot JT |title=Diva vaccines that reduce virus transmission. |journal=J. Biotechnol. |volume=73 |issue= 2-3 |pages= 195–205 |year= 1999 |pmid= 10486928 |doi=10.1016/S0168-1656(99)00121-2
*cite journal | author=Nakajima D, Okazaki N, Yamakawa H, "et al." |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99–106 |year= 2003 |pmid= 12168954 |doi=10.1093/dnares/9.3.99
*cite journal | author=Campioni M, Santini D, Tonini G, "et al." |title=Role of Apaf-1, a key regulator of apoptosis, in melanoma progression and chemoresistance. |journal=Exp. Dermatol. |volume=14 |issue= 11 |pages= 811–8 |year= 2006 |pmid= 16232302 |doi= 10.1111/j.1600-0625.2005.00360.x
*cite journal | author=Zou H, Henzel WJ, Liu X, "et al." |title=Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. |journal=Cell |volume=90 |issue= 3 |pages= 405–13 |year= 1997 |pmid= 9267021 |doi=10.1016/S0092-8674(00)80501-2
*cite journal | author=Li P, Nijhawan D, Budihardjo I, "et al." |title=Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. |journal=Cell |volume=91 |issue= 4 |pages= 479–89 |year= 1997 |pmid= 9390557 |doi=10.1016/S0092-8674(00)80434-1
*cite journal | author=Ishikawa K, Nagase T, Nakajima D, "et al." |title=Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=4 |issue= 5 |pages= 307–13 |year= 1998 |pmid= 9455477 |doi=10.1093/dnares/4.5.307
*cite journal | author=Pan G, O'Rourke K, Dixit VM |title=Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5841–5 |year= 1998 |pmid= 9488720 |doi=10.1074/jbc.273.10.5841
*cite journal | author=Hu Y, Benedict MA, Wu D, "et al." |title=Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 8 |pages= 4386–91 |year= 1998 |pmid= 9539746 |doi=10.1073/pnas.95.8.4386
*cite journal | author=Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Alnemri ES |title=Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. |journal=Mol. Cell |volume=1 |issue= 7 |pages= 949–57 |year= 1998 |pmid= 9651578 |doi=10.1016/S1097-2765(00)80095-7
*cite journal | author=Cecconi F, Alvarez-Bolado G, Meyer BI, "et al." |title=Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. |journal=Cell |volume=94 |issue= 6 |pages= 727–37 |year= 1998 |pmid= 9753320 |doi=10.1016/S0092-8674(00)81732-8
*cite journal | author=Inohara N, Gourley TS, Carrio R, "et al." |title=Diva, a Bcl-2 homologue that binds directly to Apaf-1 and induces BH3-independent cell death. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32479–86 |year= 1999 |pmid= 9829980 |doi=10.1074/jbc.273.49.32479
*cite journal | author=Hu Y, Ding L, Spencer DM, Núñez G |title=WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. |journal=J. Biol. Chem. |volume=273 |issue= 50 |pages= 33489–94 |year= 1999 |pmid= 9837928 |doi=10.1074/jbc.273.50.33489
*cite journal | author=Song Q, Kuang Y, Dixit VM, Vincenz C |title=Boo, a novel negative regulator of cell death, interacts with Apaf-1. |journal=Embo J. |volume=18 |issue= 1 |pages= 167–78 |year= 1999 |pmid= 9878060 |doi= 10.1093/emboj/18.1.167
*cite journal | author=Slee EA, Harte MT, Kluck RM, "et al." |title=Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner. |journal=J. Cell Biol. |volume=144 |issue= 2 |pages= 281–92 |year= 1999 |pmid= 9922454 |doi=10.1083/jcb.144.2.281
*cite journal | author=Zou H, Li Y, Liu X, Wang X |title=An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11549–56 |year= 1999 |pmid= 10206961 |doi=10.1074/jbc.274.17.11549
*cite journal | author=Saleh A, Srinivasula SM, Acharya S, "et al." |title=Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. |journal=J. Biol. Chem. |volume=274 |issue= 25 |pages= 17941–5 |year= 1999 |pmid= 10364241 |doi=10.1074/jbc.274.25.17941
*cite journal | author=Qin H, Srinivasula SM, Wu G, "et al." |title=Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. |journal=Nature |volume=399 |issue= 6736 |pages= 549–57 |year= 1999 |pmid= 10376594 |doi= 10.1038/21124
*cite journal | author=Drosopoulos NE, Walsh FS, Doherty P |title=A soluble version of the receptor-like protein tyrosine phosphatase kappa stimulates neurite outgrowth via a Grb2/MEK1-dependent signaling cascade. |journal=Mol. Cell. Neurosci. |volume=13 |issue= 6 |pages= 441–9 |year= 1999 |pmid= 10383829 |doi= 10.1006/mcne.1999.0758

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