Here we extend these early studies and define that PfCK2 is a dual specificity protein kinase able to phosphorylate both serine and tyrosine residues. A more detailed analysis of the potential role of PfCK2 in the nucleus has identified a number of interacting partners and substrate nuclear proteins involved in chromatin assembly and dynamics. This is supported by the wide distribution of PfCK2 in the cytoplasm and nucleus of the parasite.

It seems likely that the essential nature of PfCK2 reflects a broad regulatory role similar to that of the mammalian orthologue. falciparum through the erythrocytic life cycle. Reverse genetic studies have determined that not only the catalytic subunit for PfCK2, but also each of the regulatory ОІ-subunits, are essential for the survival of P. falciparum a single О±-subunit catalytic gene has been identified and two genes encoding the regulatory subunits (ОІ 1 and ОІ 2). The mammalian enzyme is a tetramer consisting of two catalytic subunits, for which two different genes (О± and О±вЂІ) are present in the genome, and two regulatory ОІ-subunits, derived from a single gene. Mammalian protein kinase CK2 is a pleiotropic serine/threonine protein kinase know to act on hundreds of cellular substrates involved in crucial cellular processes such as differentiation, proliferation, apoptosis, stress response, DNA damage and circadian rhythm. falciparum orthologue to protein kinase CK2, PfCK2. falciparum protein kinases that do have counterparts in the mammalian kinome. Despite this diversity it is possible to identify some P. Although many of the Plasmodium protein kinases fall into established kinase groups such as AGC and CMGC (Hanks 2003), they tend to show significant diversity from mammalian species reflecting the fact that malaria parasites in the Apicomplexan phylum branched very early in the eukaryotic lineage. Bioinformatic studies have identified 85вЂ“99 protein kinases in the Plasmodium falciparum kinome. One reason for this is the paucity of basic understanding of parasite protein kinases. Furthermore, we generate an homology model of PfCK2 in complex with the known selective protein kinase CK2 inhibitor, quinalizarin, and in so doing identify key co-ordinating residues in the ATP binding pocket that could aid in designing selective inhibitors to PfCK2.Дespite the fact that protein kinases constitute an important target in the development of drugs to treat human disease, in particular cancer, progress in targeting protein kinases in malaria has been slow. Phosphorylation at this site in PfCK2 is shown here to regulate the intrinsic kinase activity of PfCK2. However, unlike the human orthologue that is auto-phosphorylated on tyrosine within the activation loop, PfCK2 shows no activation loop auto-phosphorylation but rather is auto-phosphorylated at threonine 63 within subdomain I. Here we report a detailed analysis of the Plasmodium falciparum CK2, PfCK2, demonstrating that this kinase, like the mammalian orthologue, is a dual specificity kinase able to phosphorylate at both serine and tyrosine.

Casein kinase 2 (protein kinase CK2) is a conserved eukaryotic serine/theronine kinase with multiple substrates and roles in the regulation of cellular processes such as cellular stress, cell proliferation and apoptosis.

Ck2 found a new kingdom