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TPD52L2

Introduction

Tumor protein D54 is a protein that in humans is encoded by the TPD52L2 gene.[1][2]

Model organisms

Model organisms

Model organisms have been used in the study of TPD52L2 function. A conditional knockout mouse line, called Tpd52l2tm1a(KOMP)Wtsi[7][8] 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.[9][10][11]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[5][12]

Twenty two tests were carried out on mutant mice and one significant abnormality was observed: homozygous adult females displayed a decrease in body length by DEXA.[5]

Interactions

Interactions

TPD52L2 has been shown to interact with TPD52L1[1] and TPD52.[1]

References

References

  1. ↑ 1.0 1.1 1.2 Byrne JA, Nourse CR, Basset P, Gunning P (Mar 1998). “Identification of homo- and heteromeric interactions between members of the breast carcinoma-associated D52 protein family using the yeast two-hybrid system”. Oncogene. 16 (7): 873–81. doi:10.1038/sj.onc.1201604. PMID 9484778.
  2. ↑ “Entrez Gene: TPD52L2 tumor protein D52-like 2”.
  3. ↑ “DEXA data for Tpd52l2”. Wellcome Trust Sanger Institute.
  4. ↑ “Salmonella infection data for Tpd52l2″. Wellcome Trust Sanger Institute.
  5. ↑ 5.0 5.1 5.2 Gerdin, AK (2010). “The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice”. Acta Ophthalmologica. 88: 0. 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 (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.
  10. ↑ Dolgin E (2011). “Mouse library set to be knockout”. Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  11. ↑ 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.
  12. ↑ 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.
Further reading

Further reading

  • Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Byrne JA, Mattei MG, Basset P (1996). “Definition of the tumor protein D52 (TPD52) gene family through cloning of D52 homologues in human (hD53) and mouse (mD52)”. Genomics. 35 (3): 523–32. doi:10.1006/geno.1996.0393. PMID 8812487.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Nourse CR, Mattei MG, Gunning P, Byrne JA (1998). “Cloning of a third member of the D52 gene family indicates alternative coding sequence usage in D52-like transcripts”. Biochim. Biophys. Acta. 1443 (1–2): 155–68. doi:10.1016/S0167-4781(98)00211-5. PMID 9838088.
  • Wilson SH, Bailey AM, Nourse CR, Mattei MG, Byrne JA (2001). “Identification of MAL2, a novel member of the mal proteolipid family, though interactions with TPD52-like proteins in the yeast two-hybrid system”. Genomics. 76 (1–3): 81–8. doi:10.1006/geno.2001.6610. PMID 11549320.
  • Boutros R, Byrne JA (2005). “D53 (TPD52L1) is a cell cycle-regulated protein maximally expressed at the G2-M transition in breast cancer cells”. Exp. Cell Res. 310 (1): 152–65. doi:10.1016/j.yexcr.2005.07.009. PMID 16112108.
  • Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (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.
  • Barbaric D, Byth K, Dalla-Pozza L, Byrne JA (2006). “Expression of tumor protein D52-like genes in childhood leukemia at diagnosis: clinical and sample considerations”. Leuk. Res. 30 (11): 1355–63. doi:10.1016/j.leukres.2006.03.009. PMID 16620967.
  • Cao Q, Chen J, Zhu L, Liu Y, Zhou Z, Sha J, Wang S, Li J (2006). “A testis-specific and testis developmentally regulated tumor protein D52 (TPD52)-like protein TPD52L3/hD55 interacts with TPD52 family proteins”. Biochem. Biophys. Res. Commun. 344 (3): 798–806. doi:10.1016/j.bbrc.2006.03.208. PMID 16631610.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks”. Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.