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{{ | '''Death effector domain containing protein''' is a [[protein]] that in humans is encoded by the ''DEDD'' [[gene]].<ref name="pmid9774341">{{cite journal | vauthors = Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME | title = DEDD, a novel death effector domain-containing protein, targeted to the nucleolus | journal = EMBO J | volume = 17 | issue = 20 | pages = 5974–86 | date = Dec 1998 | pmid = 9774341 | pmc = 1170924 | doi = 10.1093/emboj/17.20.5974 }}</ref><ref name="pmid9832420">{{cite journal | vauthors = Leo CP, Hsu SY, McGee EA, Salanova M, Hsueh AJ | title = DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells | journal = Endocrinology | volume = 139 | issue = 12 | pages = 4839–48 | date = Dec 1998 | pmid = 9832420 | pmc = | doi = 10.1210/en.139.12.4839 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DEDD death effector domain containing| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9191| accessdate = }}</ref> | ||
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== Function == | |||
This gene encodes a protein that contains a death effector [[protein domain|domain]] (DED). DED is a [[protein–protein interaction]] domain shared by adaptors, regulators and executors of the [[programmed cell death]] pathway. [[Gene expression|Overexpression]] of this gene was shown to induce weak [[apoptosis]]. Upon stimulation, this protein was found to [[protein targeting#Protein translocation|translocate]] from cytoplasm to nucleus and colocalize with [[UBTF]], a basal factor required for [[RNA polymerase I]] transcription, in the [[nucleolus]]. At least three transcript variants encoding the same protein have been found for this gene.<ref name="entrez"/> | |||
== | == Interactions == | ||
{{protein- | DEDD has been shown to [[Protein-protein interaction|interact]] with: | ||
{{ | * [[CFLAR]],<ref name = pmid11965497/><ref name = pmid11741985/> | ||
* [[Caspase 8]],<ref name = pmid11965497>{{cite journal | vauthors = Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES | title = Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC | journal = Cell Death Differ. | volume = 9 | issue = 4 | pages = 439–47 | date = Apr 2002 | pmid = 11965497 | doi = 10.1038/sj/cdd/4401038 }}</ref><ref name = autogenerated1>{{cite journal | vauthors = Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME | title = DEDD, a novel death effector domain-containing protein, targeted to the nucleolus | journal = EMBO J. | volume = 17 | issue = 20 | pages = 5974–86 | date = Oct 1998 | pmid = 9774341 | pmc = 1170924 | doi = 10.1093/emboj/17.20.5974 }}</ref><ref name = pmid12527898>{{cite journal | vauthors = Alcivar A, Hu S, Tang J, Yang X | title = DEDD and DEDD2 associate with caspase-8/10 and signal cell death | journal = Oncogene | volume = 22 | issue = 2 | pages = 291–7 | date = Jan 2003 | pmid = 12527898 | doi = 10.1038/sj.onc.1206099 }}</ref> and | |||
* [[FADD]].<ref name = pmid9774341/><ref name = pmid11741985>{{cite journal | vauthors = Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC | title = Identification and characterization of DEDD2, a death effector domain-containing protein | journal = J. Biol. Chem. | volume = 277 | issue = 9 | pages = 7501–8 | date = Mar 2002 | pmid = 11741985 | doi = 10.1074/jbc.M110749200 }}</ref> | |||
== References == | |||
{{Reflist}} | |||
{{Clear}} | |||
== Further reading == | |||
{{Refbegin| 2}} | |||
* {{cite journal | vauthors = Park MY, Ryu SW, Kim KD, Lim JS, Lee ZW, Kim E | title = Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation | journal = Int. J. Cancer | volume = 115 | issue = 3 | pages = 412–8 | year = 2005 | pmid = 15688372 | doi = 10.1002/ijc.20857 }} | |||
* {{cite journal | vauthors = Alcivar A, Hu S, Tang J, Yang X | title = DEDD and DEDD2 associate with caspase-8/10 and signal cell death | journal = Oncogene | volume = 22 | issue = 2 | pages = 291–7 | year = 2003 | pmid = 12527898 | doi = 10.1038/sj.onc.1206099 }} | |||
* {{cite journal | vauthors = Lee JC, Schickling O, Stegh AH, Oshima RG, Dinsdale D, Cohen GM, Peter ME | title = DEDD regulates degradation of intermediate filaments during apoptosis | journal = J. Cell Biol. | volume = 158 | issue = 6 | pages = 1051–66 | year = 2002 | pmid = 12235123 | pmc = 2173221 | doi = 10.1083/jcb.200112124 }} | |||
* {{cite journal | vauthors = Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES | title = Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC | journal = Cell Death Differ. | volume = 9 | issue = 4 | pages = 439–47 | year = 2002 | pmid = 11965497 | doi = 10.1038/sj/cdd/4401038 }} | |||
* {{cite journal | vauthors = Schickling O, Stegh AH, Byrd J, Peter ME | title = Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription | journal = Cell Death Differ. | volume = 8 | issue = 12 | pages = 1157–68 | year = 2002 | pmid = 11753564 | doi = 10.1038/sj.cdd.4400928 }} | |||
* {{cite journal | vauthors = Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC | title = Identification and characterization of DEDD2, a death effector domain-containing protein | journal = J. Biol. Chem. | volume = 277 | issue = 9 | pages = 7501–8 | year = 2002 | pmid = 11741985 | doi = 10.1074/jbc.M110749200 }} | |||
{{Refend}} | |||
{{Gene-1-stub}} |
Latest revision as of 18:21, 30 August 2017
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External IDs | GeneCards: [1] | ||||||
Orthologs | |||||||
Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Death effector domain containing protein is a protein that in humans is encoded by the DEDD gene.[1][2][3]
Function
This gene encodes a protein that contains a death effector domain (DED). DED is a protein–protein interaction domain shared by adaptors, regulators and executors of the programmed cell death pathway. Overexpression of this gene was shown to induce weak apoptosis. Upon stimulation, this protein was found to translocate from cytoplasm to nucleus and colocalize with UBTF, a basal factor required for RNA polymerase I transcription, in the nucleolus. At least three transcript variants encoding the same protein have been found for this gene.[3]
Interactions
DEDD has been shown to interact with:
References
- ↑ 1.0 1.1 Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME (Dec 1998). "DEDD, a novel death effector domain-containing protein, targeted to the nucleolus". EMBO J. 17 (20): 5974–86. doi:10.1093/emboj/17.20.5974. PMC 1170924. PMID 9774341.
- ↑ Leo CP, Hsu SY, McGee EA, Salanova M, Hsueh AJ (Dec 1998). "DEFT, a novel death effector domain-containing molecule predominantly expressed in testicular germ cells". Endocrinology. 139 (12): 4839–48. doi:10.1210/en.139.12.4839. PMID 9832420.
- ↑ 3.0 3.1 "Entrez Gene: DEDD death effector domain containing".
- ↑ 4.0 4.1 Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES (Apr 2002). "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC". Cell Death Differ. 9 (4): 439–47. doi:10.1038/sj/cdd/4401038. PMID 11965497.
- ↑ 5.0 5.1 Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (Mar 2002). "Identification and characterization of DEDD2, a death effector domain-containing protein". J. Biol. Chem. 277 (9): 7501–8. doi:10.1074/jbc.M110749200. PMID 11741985.
- ↑ Stegh AH, Schickling O, Ehret A, Scaffidi C, Peterhänsel C, Hofmann TG, Grummt I, Krammer PH, Peter ME (Oct 1998). "DEDD, a novel death effector domain-containing protein, targeted to the nucleolus". EMBO J. 17 (20): 5974–86. doi:10.1093/emboj/17.20.5974. PMC 1170924. PMID 9774341.
- ↑ Alcivar A, Hu S, Tang J, Yang X (Jan 2003). "DEDD and DEDD2 associate with caspase-8/10 and signal cell death". Oncogene. 22 (2): 291–7. doi:10.1038/sj.onc.1206099. PMID 12527898.
Further reading
- Park MY, Ryu SW, Kim KD, Lim JS, Lee ZW, Kim E (2005). "Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation". Int. J. Cancer. 115 (3): 412–8. doi:10.1002/ijc.20857. PMID 15688372.
- Alcivar A, Hu S, Tang J, Yang X (2003). "DEDD and DEDD2 associate with caspase-8/10 and signal cell death". Oncogene. 22 (2): 291–7. doi:10.1038/sj.onc.1206099. PMID 12527898.
- Lee JC, Schickling O, Stegh AH, Oshima RG, Dinsdale D, Cohen GM, Peter ME (2002). "DEDD regulates degradation of intermediate filaments during apoptosis". J. Cell Biol. 158 (6): 1051–66. doi:10.1083/jcb.200112124. PMC 2173221. PMID 12235123.
- Zhan Y, Hegde R, Srinivasula SM, Fernandes-Alnemri T, Alnemri ES (2002). "Death effector domain-containing proteins DEDD and FLAME-3 form nuclear complexes with the TFIIIC102 subunit of human transcription factor IIIC". Cell Death Differ. 9 (4): 439–47. doi:10.1038/sj/cdd/4401038. PMID 11965497.
- Schickling O, Stegh AH, Byrd J, Peter ME (2002). "Nuclear localization of DEDD leads to caspase-6 activation through its death effector domain and inhibition of RNA polymerase I dependent transcription". Cell Death Differ. 8 (12): 1157–68. doi:10.1038/sj.cdd.4400928. PMID 11753564.
- Roth W, Stenner-Liewen F, Pawlowski K, Godzik A, Reed JC (2002). "Identification and characterization of DEDD2, a death effector domain-containing protein". J. Biol. Chem. 277 (9): 7501–8. doi:10.1074/jbc.M110749200. PMID 11741985.
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