DAD1

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{{Short description|Type of enzyme}}

{{Infobox_gene}}

Dolichyl-diphosphooligosaccharide—protein glycosyltransferase subunit DAD1 is an enzyme that in humans is encoded by the DAD1 gene.{{cite web | title = Entrez Gene: DAD1 defender against cell death 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1603}}

Function

DAD1, the defender against apoptotic cell death, was initially identified as a negative regulator of programmed cell death in the temperature sensitive tsBN7 cell line. The DAD1 protein disappeared in temperature-sensitive cells following a shift to the nonpermissive temperature, suggesting that loss of the DAD1 protein triggered apoptosis. DAD1 is believed to be a tightly associated subunit of oligosaccharyltransferase both in the intact membrane and in the purified enzyme, thus reflecting the essential nature of N-linked glycosylation in eukaryotes.

Interactions

DAD1 has been shown to interact with MCL1.{{cite journal | vauthors = Makishima T, Yoshimi M, Komiyama S, Hara N, Nishimoto T | title = A subunit of the mammalian oligosaccharyltransferase, DAD1, interacts with Mcl-1, one of the bcl-2 protein family | journal = J. Biochem. | volume = 128 | issue = 3 | pages = 399–405 | date = September 2000 | pmid = 10965038 | doi = 10.1093/oxfordjournals.jbchem.a022767 }}

References

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Further reading

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  • {{cite journal | vauthors = Yulug IG, See CG, Fisher EM, Ylug IG | title = The DAD1 protein, whose defect causes apoptotic cell death, maps to human chromosome 14 | journal = Genomics | volume = 26 | issue = 2 | pages = 433–5 | year = 1995 | pmid = 7601483 | doi = 10.1016/0888-7543(95)80241-D }}
  • {{cite journal | vauthors = Apte SS, Mattei MG, Seldin MF, Olsen BR | title = The highly conserved defender against the death 1 (DAD1) gene maps to human chromosome 14q11-q12 and mouse chromosome 14 and has plant and nematode homologs | journal = FEBS Lett. | volume = 363 | issue = 3 | pages = 304–6 | year = 1995 | pmid = 7737422 | doi = 10.1016/0014-5793(95)00321-Y | doi-access = | s2cid = 39270530 }}
  • {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
  • {{cite journal | vauthors = Nakashima T, Sekiguchi T, Kuraoka A, Fukushima K, Shibata Y, Komiyama S, Nishimoto T | title = Molecular cloning of a human cDNA encoding a novel protein, DAD1, whose defect causes apoptotic cell death in hamster BHK21 cells | journal = Mol. Cell. Biol. | volume = 13 | issue = 10 | pages = 6367–74 | year = 1993 | pmid = 8413235 | pmc = 364695 | doi = 10.1128/mcb.13.10.6367}}
  • {{cite journal | vauthors = Kelleher DJ, Gilmore R | title = DAD1, the defender against apoptotic cell death, is a subunit of the mammalian oligosaccharyltransferase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 10 | pages = 4994–9 | year = 1997 | pmid = 9144178 | pmc = 24619 | doi = 10.1073/pnas.94.10.4994 | bibcode = 1997PNAS...94.4994K | doi-access = free }}
  • {{cite journal | vauthors = Makishima T, Nakashima T, Nagata-Kuno K, Fukushima K, Iida H, Sakaguchi M, Ikehara Y, Komiyama S, Nishimoto T | title = The highly conserved DAD1 protein involved in apoptosis is required for N-linked glycosylation | journal = Genes Cells | volume = 2 | issue = 2 | pages = 129–41 | year = 1997 | pmid = 9167970 | doi = 10.1046/j.1365-2443.1997.1070303.x | s2cid = 25807010 | doi-access = free }}
  • {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | year = 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal | vauthors = Zhong XP, Krangel MS | title = Enhancer-blocking activity within the DNase I hypersensitive site 2 to 6 region between the TCR alpha and Dad1 genes | journal = J. Immunol. | volume = 163 | issue = 1 | pages = 295–300 | year = 1999 | doi = 10.4049/jimmunol.163.1.295 | pmid = 10384128 | doi-access = free }}
  • {{cite journal | vauthors = Makishima T, Yoshimi M, Komiyama S, Hara N, Nishimoto T | title = A subunit of the mammalian oligosaccharyltransferase, DAD1, interacts with Mcl-1, one of the bcl-2 protein family | journal = J. Biochem. | volume = 128 | issue = 3 | pages = 399–405 | year = 2000 | pmid = 10965038 | doi = 10.1093/oxfordjournals.jbchem.a022767 }}
  • {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nat. Biotechnol. | volume = 21 | issue = 5 | pages = 566–9 | year = 2003 | pmid = 12665801 | doi = 10.1038/nbt810 | s2cid = 23783563 }}
  • {{cite journal | vauthors = Shibatani T, David LL, McCormack AL, Frueh K, Skach WR | title = Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits | journal = Biochemistry | volume = 44 | issue = 16 | pages = 5982–92 | year = 2005 | pmid = 15835887 | doi = 10.1021/bi047328f }}

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