Jump to content

CDS2

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by KolbertBot (talk | contribs) at 04:23, 27 October 2017 (Bot: HTTP→HTTPS (v470)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

CDS2
Identifiers
AliasesCDS2, CDP-diacylglycerol synthase 2
External IDsOMIM: 603549; MGI: 1332236; HomoloGene: 37854; GeneCards: CDS2; OMA:CDS2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003818

NM_001291039
NM_001291040
NM_138651

RefSeq (protein)

NP_003809

NP_001277968
NP_001277969
NP_619592

Location (UCSC)Chr 20: 5.13 – 5.2 MbChr 2: 132.11 – 132.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Phosphatidate cytidylyltransferase 2 is an enzyme that in humans is encoded by the CDS2 gene.[5][6][7]

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.[8][9] 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.[10]

Model organisms

Model organisms have been used in the study of CDS2 function. A conditional knockout mouse line, called Cds2tm1a(KOMP)Wtsi[15][16] 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.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][20] 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. [13]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000101290Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058793Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Halford S, Dulai KS, Daw SC, Fitzgibbon J, Hunt DM (Nov 1998). "Isolation and chromosomal localization of two human CDP-diacylglycerol synthase (CDS) genes". Genomics. 54 (1): 140–4. doi:10.1006/geno.1998.5547. PMID 9806839.
  6. ^ Volta M, Bulfone A, Gattuso C, Rossi E, Mariani M, Consalez GG, Zuffardi O, Ballabio A, Banfi S, Franco B (Jan 1999). "Identification and characterization of CDS2, a mammalian homolog of the Drosophila CDP-diacylglycerol synthase gene". Genomics. 55 (1): 68–77. doi:10.1006/geno.1998.5610. PMID 9889000.
  7. ^ "Entrez Gene: CDS2 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 2".
  8. ^ Nowicki M, Müller F, Frentzen M (Apr 2005). "Cardiolipin synthase of Arabidopsis thaliana". FEBS Letters. 579 (10): 2161–5. doi:10.1016/j.febslet.2005.03.007. PMID 15811335.
  9. ^ Nowicki M (2006). "Characterization of the Cardiolipin Synthase from Arabidopsis thaliana". Ph.D. thesis, RWTH-Aachen University.
  10. ^ "Entrez Gene: CDS1 CDP-diacylglycerol synthase (phosphatidate cytidylyltransferase) 1".
  11. ^ "Salmonella infection data for Cds2". Wellcome Trust Sanger Institute.
  12. ^ "Citrobacter infection data for Cds2". Wellcome Trust Sanger Institute.
  13. ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
  14. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  15. ^ "International Knockout Mouse Consortium".
  16. ^ "Mouse Genome Informatics".
  17. ^ 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 (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  18. ^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  19. ^ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  20. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Further reading

  • Lykidis A, Jackson PD, Rock CO, Jackowski S (Dec 1997). "The role of CDP-diacylglycerol synthetase and phosphatidylinositol synthase activity levels in the regulation of cellular phosphatidylinositol content". The Journal of Biological Chemistry. 272 (52): 33402–9. doi:10.1074/jbc.272.52.33402. PMID 9407135.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  • Halford S, Inglis S, Gwilliam R, Spencer P, Mohamed M, Ebenezer ND, Hunt DM (Nov 2002). "Genomic organization of human CDS2 and evaluation as a candidate gene for corneal hereditary endothelial dystrophy 2 on chromosome 20p13". Experimental Eye Research. 75 (5): 619–23. doi:10.1006/exer.2002.2052. PMID 12457874.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.