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DFFB

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DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)
PDB rendering based on 1ibx.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols DFFB ; CAD; CPAN; DFF-40; DFF2; DFF40
External IDs Template:OMIM5 Template:MGI HomoloGene: 3241
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase), also known as DFFB, is a human gene.[1]

Apoptosis is a cell death process that removes toxic and/or useless cells during mammalian development. The apoptotic process is accompanied by shrinkage and fragmentation of the cells and nuclei and degradation of the chromosomal DNA into nucleosomal units. DNA fragmentation factor (DFF) is a heterodimeric protein of 40-kD (DFFB) and 45-kD (DFFA) subunits. DFFA is the substrate for caspase-3 and triggers DNA fragmentation during apoptosis. DFF becomes activated when DFFA is cleaved by caspase-3. The cleaved fragments of DFFA dissociate from DFFB, the active component of DFF. DFFB has been found to trigger both DNA fragmentation and chromatin condensation during apoptosis. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the biological validity of some variants has not been determined.[1]

References[edit | edit source]

  1. ↑ 1.0 1.1 "Entrez Gene: DFFB DNA fragmentation factor, 40kDa, beta polypeptide (caspase-activated DNase)".

Further reading[edit | edit source]

  • Liu X, Zou H, Slaughter C, Wang X (1997). "DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis". Cell. 89 (2): 175–84. PMID 9108473.
  • Enari M, Sakahira H, Yokoyama H; et al. (1998). "A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD". Nature. 391 (6662): 43–50. doi:10.1038/34112. PMID 9422506.
  • Halenbeck R, MacDonald H, Roulston A; et al. (1998). "CPAN, a human nuclease regulated by the caspase-sensitive inhibitor DFF45". Curr. Biol. 8 (9): 537–40. PMID 9560346.
  • Liu X, Li P, Widlak P; et al. (1998). "The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8461–6. PMID 9671700.
  • Mukae N, Enari M, Sakahira H; et al. (1998). "Molecular cloning and characterization of human caspase-activated DNase". Proc. Natl. Acad. Sci. U.S.A. 95 (16): 9123–8. PMID 9689044.
  • Gu J, Dong RP, Zhang C; et al. (1999). "Functional interaction of DFF35 and DFF45 with caspase-activated DNA fragmentation nuclease DFF40". J. Biol. Chem. 274 (30): 20759–62. PMID 10409614.
  • McCarty JS, Toh SY, Li P (1999). "Study of DFF45 in its role of chaperone and inhibitor: two independent inhibitory domains of DFF40 nuclease activity". Biochem. Biophys. Res. Commun. 264 (1): 176–80. doi:10.1006/bbrc.1999.1497. PMID 10527860.
  • McCarty JS, Toh SY, Li P (1999). "Multiple domains of DFF45 bind synergistically to DFF40: roles of caspase cleavage and sequestration of activator domain of DFF40". Biochem. Biophys. Res. Commun. 264 (1): 181–5. doi:10.1006/bbrc.1999.1498. PMID 10527861.
  • Lugovskoy AA, Zhou P, Chou JJ; et al. (2000). "Solution structure of the CIDE-N domain of CIDE-B and a model for CIDE-N/CIDE-N interactions in the DNA fragmentation pathway of apoptosis". Cell. 99 (7): 747–55. PMID 10619428.
  • Judson H, van Roy N, Strain L; et al. (2000). "Structure and mutation analysis of the gene encoding DNA fragmentation factor 40 (caspase-activated nuclease), a candidate neuroblastoma tumour suppressor gene". Hum. Genet. 106 (4): 406–13. PMID 10830907.
  • Otomo T, Sakahira H, Uegaki K; et al. (2000). "Structure of the heterodimeric complex between CAD domains of CAD and ICAD". Nat. Struct. Biol. 7 (8): 658–62. doi:10.1038/77957. PMID 10932250.
  • Durrieu F, Samejima K, Fortune JM; et al. (2001). "DNA topoisomerase IIalpha interacts with CAD nuclease and is involved in chromatin condensation during apoptotic execution". Curr. Biol. 10 (15): 923–6. PMID 10959840.
  • Zhou P, Lugovskoy AA, McCarty JS; et al. (2001). "Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45". Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6051–5. doi:10.1073/pnas.111145098. PMID 11371636.
  • Nie Z, Phenix BN, Lum JJ; et al. (2003). "HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation". Cell Death Differ. 9 (11): 1172–84. doi:10.1038/sj.cdd.4401094. PMID 12404116.
  • 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. PMID 12477932.
  • Hsieh SY, Liaw SF, Lee SN; et al. (2003). "Aberrant caspase-activated DNase (CAD) transcripts in human hepatoma cells". Br. J. Cancer. 88 (2): 210–6. doi:10.1038/sj.bjc.6600695. PMID 12610505.
  • Liu QL, Kishi H, Ohtsuka K, Muraguchi A (2003). "Heat shock protein 70 binds caspase-activated DNase and enhances its activity in TCR-stimulated T cells". Blood. 102 (5): 1788–96. doi:10.1182/blood-2002-11-3499. PMID 12738667.
  • Widlak P, Lanuszewska J, Cary RB, Garrard WT (2003). "Subunit structures and stoichiometries of human DNA fragmentation factor proteins before and after induction of apoptosis". J. Biol. Chem. 278 (29): 26915–22. doi:10.1074/jbc.M303807200. PMID 12748178.
  • Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMID 14759258.
  • Bayascas JR, Yuste VJ, Solé C; et al. (2004). "Characterization of splice variants of human caspase-activated DNase with CIDE-N structure and function". FEBS Lett. 566 (1–3): 234–40. doi:10.1016/j.febslet.2004.04.050. PMID 15147901.

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