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SYMPK

Introduction

Symplekin is a protein that in humans is encoded by the SYMPK gene.[1][2]

Function

Function

This gene encodes a nuclear protein that functions in the regulation of polyadenylation and promotes gene expression. The protein forms a high-molecular weight complex with components of the polyadenylation machinery. It is thought to serve as a scaffold for recruiting regulatory factors to the polyadenylation complex. It also participates in 3′-end maturation of histone mRNAs, which do not undergo polyadenylation. The protein also localizes to the cytoplasmic plaques of tight junctions in some cell types.[2]

Model organisms

Model organisms

Model organisms have been used in the study of SYMPK function. A conditional knockout mouse line, called Sympktm1a(EUCOMM)Wtsi[7][8] was generated as part of the International Knockout Mouse Consortium program β€” a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[9][10][11]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[5][12] Twenty five tests were carried out on mutant mice and two significant abnormalities were observed.[5] 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; no additional significant abnormalities were observed in these animals.[5]

Interactions

Interactions

SYMPK has been shown to interact with CSTF2[13] and HSF1.[14]

References

References

  1. ↑ Ueki K, Ramaswamy S, Billings SJ, Mohrenweiser HW, Louis DN (May 1997). “Chromosomal localization to 19q13.3, partial genomic structure and 5′ cDNA sequence of the human symplekin gene”. Somatic Cell and Molecular Genetics. 23 (3): 229–31. doi:10.1007/BF02721375. PMIDΒ 9330635.
  2. ↑ 2.0 2.1 “Entrez Gene: SYMPK symplekin”.
  3. ↑ “Salmonella infection data for Sympk”. Wellcome Trust Sanger Institute.
  4. ↑ “Citrobacter infection data for Sympk”. Wellcome Trust Sanger Institute.
  5. ↑ 5.0 5.1 5.2 5.3 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.
  6. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  7. ↑ “International Knockout Mouse Consortium”.
  8. ↑ “Mouse Genome Informatics”.
  9. ↑ 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. PMCΒ 3572410. PMIDΒ 21677750.
  10. ↑ Dolgin E (Jun 2011). “Mouse library set to be knockout”. Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMIDΒ 21677718.
  11. ↑ 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. PMIDΒ 17218247.
  12. ↑ 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. PMCΒ 3218837. PMIDΒ 21722353.
  13. ↑ Takagaki Y, Manley JL (Mar 2000). “Complex protein interactions within the human polyadenylation machinery identify a novel component”. Molecular and Cellular Biology. 20 (5): 1515–25. doi:10.1128/MCB.20.5.1515-1525.2000. PMCΒ 85326. PMIDΒ 10669729.
  14. ↑ Xing H, Mayhew CN, Cullen KE, Park-Sarge OK, Sarge KD (Mar 2004). “HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin”. The Journal of Biological Chemistry. 279 (11): 10551–5. doi:10.1074/jbc.M311719200. PMIDΒ 14707147.
Further reading

Further reading