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词条 CDS2
释义

  1. References

  2. External links

  3. Further reading

{{for|the aerodrome using the TC LID, CDS2|Disley Aerodrome}}{{Infobox_gene}}Phosphatidate cytidylyltransferase 2 is an enzyme that in humans is encoded by the CDS2 gene.[1][2][3]

Breakdown products of phosphoinositides are ubiquitous second messengers that function downstream of many G protein-coupled receptors and tyrosine kinases regulating cell growth, calcium metabolism, and protein kinase C activity. This gene encodes an enzyme which regulates the amount of phosphatidylinositol available for signaling by catalyzing the conversion of phosphatidic acid to CDP-diacylglycerol. This enzyme is an integral membrane protein localized to two subcellular domains, the matrix side of the inner mitochondrial membrane where it is thought to be involved in the synthesis of phosphatidylglycerol and cardiolipin.[4][5] and the cytoplasmic side of the endoplasmic reticulum where it functions in phosphatidylinositol biosynthesis. Two genes encoding this enzyme have been identified in humans, one mapping to human chromosome 4q21 (CDS1) and a second (this gene) to 20p13.[6]

==Model organisms==

Model organisms have been used in the study of CDS2 function. A conditional knockout mouse line, called Cds2tm1a(KOMP)Wtsi[11][12] was generated as part of the International Knockout Mouse Consortium program, a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty six tests were carried out and two phenotypes were reported. No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no significant abnormalities were observed in these animals. [9]

References

1. ^{{cite journal | vauthors = Halford S, Dulai KS, Daw SC, Fitzgibbon J, Hunt DM | title = Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes | journal = Genomics | volume = 54 | issue = 1 | pages = 140–4 | date = Nov 1998 | pmid = 9806839 | pmc = | doi = 10.1006/geno.1998.5547 }}
2. ^{{cite journal | vauthors = Volta M, Bulfone A, Gattuso C, Rossi E, Mariani M, Consalez GG, Zuffardi O, Ballabio A, Banfi S, Franco B | title = Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene | journal = Genomics | volume = 55 | issue = 1 | pages = 68–77 | date = Jan 1999 | pmid = 9889000 | pmc = | doi = 10.1006/geno.1998.5610 }}
3. ^{{cite web | title = Entrez Gene: CDS2 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8760| accessdate = }}
4. ^{{cite journal | vauthors = Nowicki M, Müller F, Frentzen M | title = Cardiolipin synthase of Arabidopsis thaliana | journal = FEBS Letters | volume = 579 | issue = 10 | pages = 2161–5 | date = Apr 2005 | pmid = 15811335 | doi = 10.1016/j.febslet.2005.03.007 }}
5. ^{{cite journal | vauthors = Nowicki M | title = Characterization of the Cardiolipin Synthase from Arabidopsis thaliana | journal = Ph.D. thesis, RWTH-Aachen University | year = 2006 | url = http://darwin.bth.rwth-aachen.de/opus/volltexte/2006/1629/}}
6. ^{{cite web | title = Entrez Gene: CDS1 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1040| accessdate = }}
7. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MADE/salmonella-challenge/ |title=Salmonella infection data for Cds2 |publisher=Wellcome Trust Sanger Institute}}
8. ^{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MADE/citrobacter-challenge/ |title=Citrobacter infection data for Cds2 |publisher=Wellcome Trust Sanger Institute}}
9. ^{{cite journal| doi = 10.1111/j.1755-3768.2010.4142.x| title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice| year = 2010| author = Gerdin AK| journal = Acta Ophthalmologica| volume = 88| issue = S248 }}
10. ^Mouse Resources Portal, Wellcome Trust Sanger Institute.
11. ^{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Cds2 |title=International Knockout Mouse Consortium}}
12. ^{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4363703 |title=Mouse Genome Informatics}}
13. ^{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | date = Jun 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}
14. ^{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | date = Jun 2011 | pmid = 21677718 | doi = 10.1038/474262a }}
15. ^{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | date = Jan 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}
16. ^{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism | journal = Genome Biology | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}

External links

  • {{UCSC gene info|CDS2}}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors = Lykidis A, Jackson PD, Rock CO, Jackowski S | title = The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content | journal = The Journal of Biological Chemistry | volume = 272 | issue = 52 | pages = 33402–9 | date = Dec 1997 | pmid = 9407135 | doi = 10.1074/jbc.272.52.33402 }}
  • {{cite journal | vauthors = Halford S, Inglis S, Gwilliam R, Spencer P, Mohamed M, Ebenezer ND, Hunt DM | title = Genomic organization of human CDS2 and evaluation as a candidate gene for corneal hereditary endothelial dystrophy 2 on chromosome 20p13 | journal = Experimental Eye Research | volume = 75 | issue = 5 | pages = 619–23 | date = Nov 2002 | pmid = 12457874 | doi = 10.1006/exer.2002.2052 }}
  • {{cite journal | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }}
{{refend}}{{Kinases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}

2 : EC 2.7.7|Genes mutated in mice

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