SMC3
Structural maintenance of chromosomes 3, also known as SMC3, is a human gene.[1]
Function
This gene belongs to the SMC3 subfamily of SMC proteins. The encoded protein occurs in certain cell types as either an intracellular, nuclear protein or a secreted protein. The nuclear form, known as structural maintenance of chromosomes 3, is a component of the multimeric cohesin complex that holds together sister chromatids during mitosis, enabling proper chromosome segregation. Post-translational modification of the encoded protein by the addition of chondroitin sulfate chains gives rise to the secreted proteoglycan bamacan, an abundant basement membrane protein.[1]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Abnormal |
| Recessive lethal study | Abnormal |
| Homozygous Fertility | Abnormal |
| Body weight | Abnormal[2] |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Abnormal[3] |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Abnormal[4] |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Haematology | Normal |
| Peripheral blood lymphocytes | Normal |
| Heart weight | 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 SMC3 function. A conditional knockout mouse line, called Smc3tm1a(EUCOMM)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 two tests were carried out on mutant mice and six significant abnormalities were observed.[7] No homozygous mutant embryos were identified during gestation, and thus none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice. Females had a higher than normal incidence of pre-wean death in their offspring, and also had a decreased body weight. Males heterozygotes displayed a shortened, upturned snout.[7][14]
Interactions
SMC3 (gene) has been shown to interact with:
See also
References
- ↑ 1.0 1.1 "Entrez Gene: SMC3 structural maintenance of chromosomes 3".
- ↑ "Body weight data for Smc3". Wellcome Trust Sanger Institute.
- ↑ "Dysmorphology data for Smc3". Wellcome Trust Sanger Institute.
- ↑ "DEXA data for Smc3". Wellcome Trust Sanger Institute.
- ↑ "Salmonella infection data for Smc3". Wellcome Trust Sanger Institute.
- ↑ "Citrobacter infection data for Smc3". Wellcome Trust Sanger Institute.
- ↑ 7.0 7.1 7.2 7.3 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 WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V et al. (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.
- ↑ 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.
- ↑ 14.0 14.1 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.
- ↑ Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (March 1998). "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide". J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
- ↑ 16.0 16.1 Gupta K, Anand G, Yin X, Grove L, Prochownik EV (March 1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
- ↑ 17.0 17.1 Lee J, Iwai T, Yokota T, Yamashita M (July 2003). "Temporally and spatially selective loss of Rec8 protein from meiotic chromosomes during mammalian meiosis". J. Cell. Sci. 116 (Pt 13): 2781–90. doi:10.1242/jcs.00495. PMID 12759374.
- ↑ Kim ST, Xu B, Kastan MB (March 2002). "Involvement of the cohesin protein, Smc1, in Atm-dependent and independent responses to DNA damage". Genes Dev. 16 (5): 560–70. doi:10.1101/gad.970602. PMC 155347. PMID 11877376.
- ↑ Schmiesing JA, Ball AR, Gregson HC, Alderton JM, Zhou S, Yokomori K (October 1998). "Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12906–11. doi:10.1073/pnas.95.22.12906. PMC 23650. PMID 9789013.
- ↑ Gregson HC, Schmiesing JA, Kim JS, Kobayashi T, Zhou S, Yokomori K (Dec 2001). "A potential role for human cohesin in mitotic spindle aster assembly". J. Biol. Chem. 276 (50): 47575–82. doi:10.1074/jbc.M103364200. PMID 11590136.
Further reading
- Wu RR, Couchman JR (1997). "cDNA cloning of the basement membrane chondroitin sulfate proteoglycan core protein, bamacan: a five domain structure including coiled-coil motifs". J. Cell Biol. 136 (2): 433–44. doi:10.1083/jcb.136.2.433. PMC 2134808. PMID 9015313.
- Shimizu K, Shirataki H, Honda T, Minami S, Takai Y (1998). "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein, with a human chromosome-associated polypeptide". J. Biol. Chem. 273 (12): 6591–4. doi:10.1074/jbc.273.12.6591. PMID 9506951.
- Gupta K, Anand G, Yin X, Grove L, Prochownik EV (1998). "Mmip1: a novel leucine zipper protein that reverses the suppressive effects of Mad family members on c-myc". Oncogene 16 (9): 1149–59. doi:10.1038/sj.onc.1201634. PMID 9528857.
- Schmiesing JA, Ball AR, Gregson HC, Alderton JM, Zhou S, Yokomori K (1998). "Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 12906–11. doi:10.1073/pnas.95.22.12906. PMC 23650. PMID 9789013.
- Ghiselli G, Iozzo RV (2000). "Overexpression of bamacan/SMC3 causes transformation". J. Biol. Chem. 275 (27): 20235–8. doi:10.1074/jbc.C000213200. PMID 10801778.
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ et al. (2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
- Sumara I, Vorlaufer E, Gieffers C, Peters BH, Peters JM (2000). "Characterization of vertebrate cohesin complexes and their regulation in prophase". J. Cell Biol. 151 (4): 749–62. doi:10.1083/jcb.151.4.749. PMC 2169443. PMID 11076961.
- Revenkova E, Eijpe M, Heyting C, Gross B, Jessberger R (2001). "Novel meiosis-specific isoform of mammalian SMC1". Mol. Cell. Biol. 21 (20): 6984–98. doi:10.1128/MCB.21.20.6984-6998.2001. PMC 99874. PMID 11564881.
- Gregson HC, Schmiesing JA, Kim JS, Kobayashi T, Zhou S, Yokomori K (2001). "A potential role for human cohesin in mitotic spindle aster assembly". J. Biol. Chem. 276 (50): 47575–82. doi:10.1074/jbc.M103364200. PMID 11590136.
- Kim ST, Xu B, Kastan MB (2002). "Involvement of the cohesin protein, Smc1, in Atm-dependent and independent responses to DNA damage". Genes Dev. 16 (5): 560–70. doi:10.1101/gad.970602. PMC 155347. PMID 11877376.
- James RD, Schmiesing JA, Peters AH, Yokomori K, Disteche CM (2002). "Differential association of SMC1alpha and SMC3 proteins with meiotic chromosomes in wild-type and SPO11-deficient male mice". Chromosome Res. 10 (7): 549–60. doi:10.1023/A:1020910601858. PMID 12498344.
- Ghiselli G, Coffee N, Munnery CE, Koratkar R, Siracusa LD (2003). "The cohesin SMC3 is a target the for beta-catenin/TCF4 transactivation pathway". J. Biol. Chem. 278 (22): 20259–67. doi:10.1074/jbc.M209511200. PMID 12651860.
- Lee J, Iwai T, Yokota T, Yamashita M (2003). "Temporally and spatially selective loss of Rec8 protein from meiotic chromosomes during mammalian meiosis". J. Cell. Sci. 116 (Pt 13): 2781–90. doi:10.1242/jcs.00495. PMID 12759374.
- Prieto I, Tease C, Pezzi N, Buesa JM, Ortega S, Kremer L et al. (2004). "Cohesin component dynamics during meiotic prophase I in mammalian oocytes". Chromosome Res. 12 (3): 197–213. doi:10.1023/B:CHRO.0000021945.83198.0e. PMID 15125634.
- Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI et al. (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Patel CA, Ghiselli G (2005). "Hinderin, a five-domains protein including coiled-coil motifs that binds to SMC3". BMC Cell Biol. 6 (1): 3. doi:10.1186/1471-2121-6-3. PMC 547899. PMID 15656913.
- Rankin S, Ayad NG, Kirschner MW (2005). "Sororin, a substrate of the anaphase-promoting complex, is required for sister chromatid cohesion in vertebrates". Mol. Cell 18 (2): 185–200. doi:10.1016/j.molcel.2005.03.017. PMID 15837422.
- Khanna H, Hurd TW, Lillo C, Shu X, Parapuram SK, He S et al. (2005). "RPGR-ORF15, which is mutated in retinitis pigmentosa, associates with SMC1, SMC3, and microtubule transport proteins". J. Biol. Chem. 280 (39): 33580–7. doi:10.1074/jbc.M505827200. PMC 1249479. PMID 16043481.
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