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Gene Review

Tb927.3.1630  -  casein kinase 1

Trypanosoma brucei brucei strain 927/4 GUTat10.1

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Disease relevance of Tb927.3.1630

  • L. major CK1 isoform 2 expressed as a recombinant protein in Escherichia coli displayed biochemical and inhibition characteristics similar to those of the purified native enzyme [1].

High impact information on Tb927.3.1630

  • Since the casein-kinase-like activity is higher in the slender than in the stumpy forms, the enhanced phosphorylation of pp42 and pp37 in the non-dividing parasites is probably a result of the enhanced synthesis of these acidic proteins [2].
  • Biochemical studies have led to the unexpected discovery that an isoform of CK1 represents the primary target of the pyrrole and imidazopyridine kinase inhibitors in these organisms [1].
  • Casein kinase 1 (CK1) is a family of multifunctional Ser/Thr protein kinases that are ubiquitous in eukaryotic cells [1].

Analytical, diagnostic and therapeutic context of Tb927.3.1630

  • The results described here warrant further evaluation of the activity of these kinase inhibitors against mammalian stage Leishmania parasites in vitro and in animal models of infection, as well as studies to genetically validate CK1 as a therapeutic target in trypanosomatid parasites [1].
  • Further purification of CK1 activity from L. major and characterization via liquid chromatography coupled tandem mass spectrometry identified CK1 isoform 2 as the specific parasite protein inhibited by imidazopyridines [1].


  1. Inhibitors of casein kinase 1 block the growth of Leishmania major promastigotes in vitro. Allocco, J.J., Donald, R., Zhong, T., Lee, A., Tang, Y.S., Hendrickson, R.C., Liberator, P., Nare, B. Int. J. Parasitol. (2006) [Pubmed]
  2. Phosphorylation differences among proteins of bloodstream developmental stages of Trypanosoma brucei brucei. Aboagye-Kwarteng, T., ole-MoiYoi, O.K., Lonsdale-Eccles, J.D. Biochem. J. (1991) [Pubmed]
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