AMFR
| View/Edit Human | View/Edit Mouse |
Autocrine motility factor receptor, isoform 2 is a protein that in humans is encoded by the AMFR gene.[3][4]
Autocrine motility factor is a tumor motility-stimulating protein secreted by tumor cells. The protein encoded by this gene is a glycosylated transmembrane protein and a receptor for autocrine motility factor. The receptor, which shows some sequence similarity to tumor protein p53, is localized to the leading and trailing edges of carcinoma cells.[4]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Abnormal |
| Recessive lethal study | Normal |
| Fertility | Normal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Plasma immunoglobulins | Normal |
| Haematology | Normal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Skin Histopathology | Normal |
| Brain histopathology | Normal |
| Eye Histopathology | Normal |
| Salmonella infection | Normal[5] |
| Citrobacter infection | Normal[6] |
| All tests and analysis from[7][8] |
Model organisms have been used in the study of AMFR function. A conditional knockout mouse line, called Amfrtm1a(KOMP)Wtsi[9][10] 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.[11][12][13]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] Twenty six tests were carried out on mutant mice and one significant abnormality was observed: Fewer than expected homozygous mutant mice survived until weaning.[7]
Interactions
AMFR has been shown to interact with Valosin-containing protein.[15][16]
References
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Watanabe H, Carmi P, Hogan V, Raz T, Silletti S, Nabi IR, Raz A (Aug 1991). "Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor". J Biol Chem. 266 (20): 13442–8. PMID 1649192.
- 1 2 "Entrez Gene: AMFR autocrine motility factor receptor".
- ↑ "Salmonella infection data for Amfr". Wellcome Trust Sanger Institute.
- ↑ "Citrobacter infection data for Amfr". Wellcome Trust Sanger Institute.
- 1 2 3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ↑ "International Knockout Mouse Consortium".
- ↑ "Mouse Genome Informatics".
- ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410
. PMID 21677750. - ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ↑ Collins FS, Rossant J, Wurst W (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. PMC 3218837. PMID 21722353.
- ↑ Zhong, Xiaoyan; Shen Yuxian; Ballar Petek; Apostolou Andria; Agami Reuven; Fang Shengyun (Oct 2004). "AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation". J. Biol. Chem. United States. 279 (44): 45676–84. doi:10.1074/jbc.M409034200. ISSN 0021-9258. PMID 15331598.
- ↑ Lee, Joon No; Zhang Xiangyu; Feramisco Jamison D; Gong Yi; Ye Jin (Nov 2008). "Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step". J. Biol. Chem. United States. 283 (48): 33772–83. doi:10.1074/jbc.M806108200. ISSN 0021-9258. PMC 2586246. PMID 18835813.
Further reading
- Huang B, Xie Y, Raz A (1995). "Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor.". Biochem. Biophys. Res. Commun. 212 (3): 727–42. doi:10.1006/bbrc.1995.2031. PMID 7626106.
- Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags.". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
- Shimizu K, Tani M, Watanabe H, et al. (1999). "The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein.". FEBS Lett. 456 (2): 295–300. doi:10.1016/S0014-5793(99)00966-7. PMID 10456327.
- Fang S, Ferrone M, Yang C, et al. (2002). "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.". Proc. Natl. Acad. Sci. U.S.A. 98 (25): 14422–7. doi:10.1073/pnas.251401598. PMC 64697. PMID 11724934.
- Luo Y, Long JM, Lu C, et al. (2002). "A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78.". J. Neurochem. 80 (2): 354–61. doi:10.1046/j.0022-3042.2001.00707.x. PMID 11902125.
- Tímár J, Rásó E, Döme B, et al. (2002). "Expression and function of the AMF receptor by human melanoma in experimental and clinical systems.". Clin. Exp. Metastasis. 19 (3): 225–32. doi:10.1023/A:1015595708241. PMID 12067203.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Liang JS, Kim T, Fang S, et al. (2003). "Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells.". J. Biol. Chem. 278 (26): 23984–8. doi:10.1074/jbc.M302683200. PMID 12670940.
- Takanami I, Takeuchi K (2003). "Autocrine motility factor-receptor gene expression in lung cancer.". Jpn. J. Thorac. Cardiovasc. Surg. 51 (8): 368–73. doi:10.1007/BF02719469. PMID 12962414.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Registre M, Goetz JG, St Pierre P, et al. (2004). "The gene product of the gp78/AMFR ubiquitin E3 ligase cDNA is selectively recognized by the 3F3A antibody within a subdomain of the endoplasmic reticulum.". Biochem. Biophys. Res. Commun. 320 (4): 1316–22. doi:10.1016/j.bbrc.2004.06.089. PMID 15303277.
- Zhong X, Shen Y, Ballar P, et al. (2004). "AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation.". J. Biol. Chem. 279 (44): 45676–84. doi:10.1074/jbc.M409034200. PMID 15331598.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Song BL, Sever N, DeBose-Boyd RA (2005). "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase.". Mol. Cell. 19 (6): 829–40. doi:10.1016/j.molcel.2005.08.009. PMID 16168377.
- Kaynak K, Kara M, Oz B, et al. (2006). "Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas.". Acta Chir. Belg. 105 (4): 378–82. PMID 16184720.
- Ye Y, Shibata Y, Kikkert M, et al. (2006). "Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. doi:10.1073/pnas.0505006102. PMC 1242302. PMID 16186510.
- Chen B, Mariano J, Tsai YC, et al. (2006). "The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site.". Proc. Natl. Acad. Sci. U.S.A. 103 (2): 341–6. doi:10.1073/pnas.0506618103. PMC 1326157. PMID 16407162.
- Haga A, Tanaka N, Funasaka T, et al. (2006). "The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF.". J. Mol. Biol. 358 (3): 741–53. doi:10.1016/j.jmb.2006.02.046. PMID 16563432.
- Shen Y, Ballar P, Fang S (2006). "Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin.". Biochem. Biophys. Res. Commun. 349 (4): 1285–93. doi:10.1016/j.bbrc.2006.08.173. PMID 16979136.
This article is issued from Wikipedia - version of the 5/22/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.