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词条 DPM1
释义

  1. Function

  2. Model organisms

  3. References

  4. Further reading

  5. External links

{{Infobox_gene}}Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.[1][2][3]

Function

Dolichol-phosphate mannose (Dol-P-Man) serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. Human DPM1 lacks a carboxy-terminal transmembrane domain and signal sequence and is regulated by DPM2.[3]

Model organisms

Model organisms have been used in the study of DPM1 function. A conditional knockout mouse line called Dpm1tm1b(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[4] Male and female animals underwent a standardized phenotypic screen[5] to determine the effects of deletion.[6][7][8][9] Additional screens performed: - In-depth immunological phenotyping[10]{{clear|left}}

References

1. ^{{cite journal | vauthors = Colussi PA, Taron CH, Mack JC, Orlean P | title = Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 94 | issue = 15 | pages = 7873–8 | date = Jul 1997 | pmid = 9223280 | pmc = 21522 | doi = 10.1073/pnas.94.15.7873 }}
2. ^{{cite journal | vauthors = Tomita S, Inoue N, Maeda Y, Ohishi K, Takeda J, Kinoshita T | title = A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells | journal = The Journal of Biological Chemistry | volume = 273 | issue = 15 | pages = 9249–54 | date = Apr 1998 | pmid = 9535917 | pmc = | doi = 10.1074/jbc.273.15.9249 }}
3. ^1 {{cite web | title = Entrez Gene: DPM1 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8813| accessdate = }}
4. ^{{cite journal |title=The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice |author=Gerdin AK |year=2010 |journal=Acta Ophthalmologica|volume=88 |pages=925–7|doi=10.1111/j.1755-3768.2010.4142.x }}
5. ^1 {{cite web |url=http://www.mousephenotype.org/data/search?q=Dpm1#fq=**&facet=gene |title=International Mouse Phenotyping Consortium}}
6. ^{{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 }}
7. ^{{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 }}
8. ^{{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 }}
9. ^{{cite journal | vauthors = White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP | title = Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes | journal = Cell | volume = 154 | issue = 2 | pages = 452–64 | date = Jul 2013 | pmid = 23870131 | pmc = 3717207 | doi = 10.1016/j.cell.2013.06.022 }}
10. ^1 {{cite web |url= http://www.immunophenotyping.org/data/search?keys=Dpm1&field_gene_construct_tid=All |title=Infection and Immunity Immunophenotyping (3i) Consortium}}

Further reading

{{refbegin | 2}}
  • {{cite journal | vauthors = Maeda Y, Tomita S, Watanabe R, Ohishi K, Kinoshita T | title = DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate | journal = The EMBO Journal | volume = 17 | issue = 17 | pages = 4920–9 | date = Sep 1998 | pmid = 9724629 | pmc = 1170821 | doi = 10.1093/emboj/17.17.4920 }}
  • {{cite journal | vauthors = Kim S, Westphal V, Srikrishna G, Mehta DP, Peterson S, Filiano J, Karnes PS, Patterson MC, Freeze HH | title = Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie) | journal = The Journal of Clinical Investigation | volume = 105 | issue = 2 | pages = 191–8 | date = Jan 2000 | pmid = 10642597 | pmc = 377427 | doi = 10.1172/JCI7302 }}
  • {{cite journal | vauthors = Imbach T, Schenk B, Schollen E, Burda P, Stutz A, Grunewald S, Bailie NM, King MD, Jaeken J, Matthijs G, Berger EG, Aebi M, Hennet T | title = Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie | journal = The Journal of Clinical Investigation | volume = 105 | issue = 2 | pages = 233–9 | date = Jan 2000 | pmid = 10642602 | pmc = 377434 | doi = 10.1172/JCI8691 }}
  • {{cite journal | vauthors = Maeda Y, Tanaka S, Hino J, Kangawa K, Kinoshita T | title = Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3 | journal = The EMBO Journal | volume = 19 | issue = 11 | pages = 2475–82 | date = Jun 2000 | pmid = 10835346 | pmc = 212771 | doi = 10.1093/emboj/19.11.2475 }}
  • {{cite journal | vauthors = García-Silva MT, Matthijs G, Schollen E, Cabrera JC, Sanchez del Pozo J, Martí Herreros M, Simón R, Maties M, Martín Hernández E, Hennet T, Briones P | title = Congenital disorder of glycosylation (CDG) type Ie. A new patient | journal = Journal of Inherited Metabolic Disease | volume = 27 | issue = 5 | pages = 591–600 | year = 2005 | pmid = 15669674 | doi = 10.1023/B:BOLI.0000042984.42433.d8 }}
  • {{cite journal | vauthors = Ashida H, Maeda Y, Kinoshita T | title = DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3 | journal = The Journal of Biological Chemistry | volume = 281 | issue = 2 | pages = 896–904 | date = Jan 2006 | pmid = 16280320 | doi = 10.1074/jbc.M511311200 }}
  • {{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 }}
  • {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Molecular Systems Biology | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
{{refend}}

External links

  • [https://www.ncbi.nlm.nih.gov/books/NBK1332/ GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
{{Glycosyltransferases}}{{gene-20-stub}}
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