AIFM1

Apoptosis-inducing factor, mitochondrion-associated, 1
PDB rendering based on 1gv4.
Available structures PDB 1gv4, 1m6i
Identifiers
Symbols	AIFM1; AIF; COXPD6; MGC111425; PDCD8
External IDs	OMIM: 300169 MGI: 1349419 HomoloGene: 3100 GeneCards: AIFM1 Gene
Gene Ontology Molecular function • DNA binding • protein binding • electron carrier activity • oxidoreductase activity • flavin adenine dinucleotide binding Cellular component • soluble fraction • nucleus • cytoplasm • mitochondrion • mitochondrial inner membrane • mitochondrial intermembrane space • microsome • cytosol • membrane • perinuclear region of cytoplasm Biological process • DNA fragmentation involved in apoptotic nuclear change • activation of caspase activity • DNA damage response, signal transduction resulting in induction of apoptosis • cell redox homeostasis • neuron apoptosis • apoptosis in response to endoplasmic reticulum stress Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9131	26926
Ensembl	ENSG00000156709	ENSMUSG00000036932
UniProt	O95831	Q1L6K5
RefSeq (mRNA)	NM_001130846.2	NM_012019.2
RefSeq (protein)	NP_001124318.1	NP_036149.1
Location (UCSC)	Chr X: 129.26 – 129.3 Mb	Chr X: 45.83 – 45.87 Mb
PubMed search	[1]	[2]

Apoptosis-inducing factor 1, mitochondrial is a protein that in humans is encoded by the AIFM1 gene.

This gene encodes a flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. Induction of apoptosis results in the translocation of this protein to the nucleus where it effects chromosome condensation and fragmentation. In addition, this gene product induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. Three alternative transcripts encoding different isoforms have been identified for this gene.

Interactions

AIFM1 has been shown to interact with HSPA1A.

Further reading

• Daugas E, Nochy D, Ravagnan L, et al. (2000). "Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis". FEBS Lett. 476 (3): 118–23. doi:10.1016/S0014-5793(00)01731-2. PMID 10913597. 
• Ferri KF, Jacotot E, Blanco J, et al. (2001). "Mitochondrial control of cell death induced by HIV-1-encoded proteins". Ann. N. Y. Acad. Sci. 926: 149–64. doi:10.1111/j.1749-6632.2000.tb05609.x. PMID 11193032. 
• Candé C, Cohen I, Daugas E, et al. (2002). "Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria". Biochimie 84 (2–3): 215–22. doi:10.1016/S0300-9084(02)01374-3. PMID 12022952. 
• Castedo M, Perfettini JL, Andreau K, et al. (2004). "Mitochondrial apoptosis induced by the HIV-1 envelope". Ann. N. Y. Acad. Sci. 1010: 19–28. doi:10.1196/annals.1299.004. PMID 15033690. 
• Moon HS, Yang JS (2006). "Role of HIV Vpr as a regulator of apoptosis and an effector on bystander cells". Mol. Cells 21 (1): 7–20. PMID 16511342. 
• Glass L (1976). "Classification of biological networks by their qualitative dynamics". J. Theor. Biol. 54 (1): 85–107. doi:10.1016/S0022-5193(75)80056-7. PMID 1202295. 
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474. 
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146. 
• Susin SA, Zamzami N, Castedo M, et al. (1997). "The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis". J. Exp. Med. 186 (1): 25–37. doi:10.1084/jem.186.1.25. PMC 2198951. PMID 9206994. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2198951. 
• Susin SA, Lorenzo HK, Zamzami N, et al. (1999). "Mitochondrial release of caspase-2 and -9 during the apoptotic process". J. Exp. Med. 189 (2): 381–94. doi:10.1084/jem.189.2.381. PMC 2192979. PMID 9892620. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2192979. 
• Daugas E, Susin SA, Zamzami N, et al. (2000). "Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis". FASEB J. 14 (5): 729–39. PMID 10744629. 
• Joza N, Susin SA, Daugas E, et al. (2002). "Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death". Nature 410 (6828): 549–54. doi:10.1038/35069004. PMID 11279485. 
• Ravagnan L, Gurbuxani S, Susin SA, et al. (2001). "Heat-shock protein 70 antagonizes apoptosis-inducing factor". Nat. Cell Biol. 3 (9): 839–43. doi:10.1038/ncb0901-839. PMID 11533664. 
• Ye H, Cande C, Stephanou NC, et al. (2002). "DNA binding is required for the apoptogenic action of apoptosis inducing factor". Nat. Struct. Biol. 9 (9): 680–4. doi:10.1038/nsb836. PMID 12198487. 
• Roumier T, Vieira HL, Castedo M, et al. (2003). "The C-terminal moiety of HIV-1 Vpr induces cell death via a caspase-independent mitochondrial pathway". Cell Death Differ. 9 (11): 1212–9. doi:10.1038/sj.cdd.4401089. PMID 12404120. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 

External links

• AIFM1 on the Atlas of Genetics and Oncology