OSBPL9
Oxysterol binding protein-like 9 is a protein that in humans is encoded by the OSBPL9 gene.[1]
This gene encodes a member of the oxysterol-binding protein (OSBP) family, a group of intracellular lipid receptors. Most members contain an N-terminal pleckstrin homology domain and a highly conserved C-terminal OSBP-like sterol-binding domain, although some members contain only the sterol-binding domain. This family member functions as a cholesterol transfer protein that regulates Golgi structure and function. Multiple transcript variants, most of which encode distinct isoforms, have been identified. Related pseudogenes have been identified on chromosomes 3, 11 and 12.[1]
Model organisms
Model organisms have been used in the study of OSBPL9 function. A conditional knockout mouse line, called Osbpl9tm1a(KOMP)Wtsi[6][7] 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 — at the Wellcome Trust Sanger Institute.[8][9][10]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty four tests were carried out on homozygous mutant adult mice, however no significant abnormalities were observed.[4]
References
- ^ a b "Entrez Gene: oxysterol binding protein-like 9". http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=retrieve&list_uids=114883. Retrieved 2011-08-30.
- ^ "Salmonella infection data for Osbpl9". Wellcome Trust Sanger Institute. http://www.sanger.ac.uk/mouseportal/phenotyping/MAHU/salmonella-challenge/.
- ^ "Citrobacter infection data for Osbpl9". Wellcome Trust Sanger Institute. http://www.sanger.ac.uk/mouseportal/phenotyping/MAHU/citrobacter-challenge/.
- ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Opthalmologica 88: 925-7.doi:10.1111/j.1755-3768.2010.4142.x: Wiley. http://onlinelibrary.wiley.com/doi/10.1111/j.1755-3768.2010.4142.x/abstract.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ "International Knockout Mouse Consortium". http://www.knockoutmouse.org/martsearch/search?query=Osbpl9.
- ^ "Mouse Genome Informatics". http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4364325.
- ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M. et al. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMID 21677750. edit
- ^ Dolgin E (June 2011). "Mouse library set to be knockout". Nature 474: 262-263. doi:10.1038/474262a. http://www.nature.com/news/2011/110615/full/474262a.html.
- ^ Collins FS, Rossant J, Wurst W (January 2007). A mouse for all reasons. Cell 128(1): 9-13. doi:10.1016/j.cell.2006.12.018 PMID 17218247.
- ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMID 21722353. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21722353.
Further reading
- Ngo M, Ridgway ND (2009). "Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function.". Mol. Biol. Cell 20 (5): 1388–99. doi:10.1091/mbc.E08-09-0905. PMID 19129476.
- Gauci S, Helbig AO, Slijper M, et al. (2009). "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.". Anal. Chem. 81 (11): 4493–501. doi:10.1021/ac9004309. PMID 19413330.
- Perttil? J, Merikanto K, Naukkarinen J, et al. (2009). "OSBPL10, a novel candidate gene for high triglyceride trait in dyslipidemic Finnish subjects, regulates cellular lipid metabolism.". J. Mol. Med. 87 (8): 825–35. doi:10.1007/s00109-009-0490-z. PMID 19554302.
- Chen T, Huang Z, Wang L, et al. (2009). "MicroRNA-125a-5p partly regulates the inflammatory response, lipid uptake, and ORP9 expression in oxLDL-stimulated monocyte/macrophages.". Cardiovasc. Res. 83 (1): 131–9. doi:10.1093/cvr/cvp121. PMID 19377067.
- Wyles JP, Ridgway ND (2004). "VAMP-associated protein-A regulates partitioning of oxysterol-binding protein-related protein-9 between the endoplasmic reticulum and Golgi apparatus.". Exp. Cell Res. 297 (2): 533–47. doi:10.1016/j.yexcr.2004.03.052. PMID 15212954.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1356129.
- Sowa ME, Bennett EJ, Gygi SP, Harper JW (2009). "Defining the human deubiquitinating enzyme interaction landscape.". Cell 138 (2): 389–403. doi:10.1016/j.cell.2009.04.042. PMC 2716422. PMID 19615732. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2716422.
- Talmud PJ, Drenos F, Shah S, et al. (2009). "Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.". Am. J. Hum. Genet. 85 (5): 628–42. doi:10.1016/j.ajhg.2009.10.014. PMC 2775832. PMID 19913121. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2775832.
- Lessmann E, Ngo M, Leitges M, et al. (2007). "Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation.". Cell. Signal. 19 (2): 384–92. doi:10.1016/j.cellsig.2006.07.009. PMID 16962287.
- Jaworski CJ, Moreira E, Li A, et al. (2001). "A family of 12 human genes containing oxysterol-binding domains.". Genomics 78 (3): 185–96. doi:10.1006/geno.2001.6663. PMID 11735225.
- Lehto M, Laitinen S, Chinetti G, et al. (2001). "The OSBP-related protein family in humans.". J. Lipid Res. 42 (8): 1203–13. PMID 11483621.
- Zhou Y, Li S, M?yr?np?? MI, et al. (2010). "OSBP-related protein 11 (ORP11) dimerizes with ORP9 and localizes at the Golgi-late endosome interface.". Exp. Cell Res. 316 (19): 3304–16. doi:10.1016/j.yexcr.2010.06.008. PMID 20599956.
- Bailey SD, Xie C, Do R, et al. (2010). "Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.". Diabetes Care 33 (10): 2250–3. doi:10.2337/dc10-0452. PMC 2945168. PMID 20628086. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2945168.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.