Control of simian virus 40 DNA replication by the HeLa cell nuclear kinase casein kinase I.

Cegielska, A; Virshup, David M.

doi:10.1128/mcb.13.2.1202

Cited by 64 publications

(71 citation statements)

References 46 publications

(37 reference statements)

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“…A distinction between transla- tional and post-translation regulations will ideally require the use of a specific anti-PfCK1 antibody, which is currently unavailable. The CK1 family of enzymes phosphorylates a variety of physiological substrates including transcription factor CREM (31), glycogen synthase (32), p53 (33), and the SV40 T antigen (34). Individual CK1 isoforms in lower eukaryotes are found in the cytoplasm as well as in the nuclei and play essential roles in the regulation of cellular morphogenesis and DNA repair (35)(36)(37).…”

Section: Discussionmentioning

confidence: 99%

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Barik

Taylor

Chakrabarti

1997

Journal of Biological Chemistry

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The cDNA for casein kinase 1 (CK1) of Plasmodium falciparum was cloned, sequenced, and expressed in bacteria. The single major open reading frame of the 1.2-kilobase pair cDNA coded for a 324-amino acid polypeptide of ϳ37 kDa, the predicted sequence of which showed strong identity with known CK1 isoforms. The purified recombinant enzyme exhibited properties characteristic of CK1, such as inhibition by CK1-7, the ability to phosphorylate a highly specific peptide substrate, and a strong preference for ATP over GTP. A casein kinase activity, partially purified from soluble extracts of P. falciparum by affinity chromatography through CK1-7 columns displayed identical properties. The activity showed a stage-specific expression in the parasite, in the order trophozoite > ring > > schizont. Northern analysis indicated the existence of two major CK1 mRNAs, 2.4 and 3.2 kilobase pairs long, the levels of which were in the order ring > schizont > trophozoite. Mutagenesis of recombinant CK1 defined important amino acid residues and their potential role in the conformation of the enzyme. The malarial CK1 appeared to be the one of the smallest and perhaps the most primitive CK1 enzymes known, containing little sequence information beyond the minimal catalytic domain.The parasitic protozoan, Plasmodium falciparum, is the causative agent of malaria throughout the world and is responsible for an annual death toll of nearly 3 million, the majority of which are children and pregnant mothers (1). However, tools available to control malaria are inadequate, and drug-resistant strains are widespread; moreover, the immediate prospect of a useful vaccine is uncertain. Thus, there is an urgent need to obtain fundamental knowledge about the various cellular processes of P. falciparum at the molecular level, so that susceptible targets can be identified. With this long-term goal in mind, we have initiated studies of the signal transduction system in P. falciparum. Since reversible protein phosphorylation and dephosphorylation constitute a major mechanism of signal transduction (2), one of our immediate goals has been to characterize the various protein kinases in P. falciparum. In this paper, we report the characterization, expression, stagespecific regulation, and mutational analysis of P. falciparum casein kinase 1 (PfCK1). 1 Casein kinase-1 and -2 (CK1 and CK2) are multipotential Ser/Thr protein kinases, originally purified from rabbit reticulocyte lysates using casein as substrate (reviewed in Refs. 3 and 4). In the subsequent years, both enzymes were shown to phosphorylate, and thus regulate, a wide variety of cellular proteins. The sequence alignment of CK1 genes of various organisms and deletion analysis of recombinant yeast CK1 have recently resulted in the delineation of the following domains in the prototype 45-kDa yeast enzyme (summarized in Refs. 5 and 6): an N-terminal catalytic domain of about 300 amino acids followed by a 12-residue stretch conserved among some forms but not in others; a hydrophilic 85-residue segment predi...

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Section: Discussionmentioning

confidence: 99%

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Barik

Taylor

Chakrabarti

1997

Journal of Biological Chemistry

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“…Also, a CKI-like activity can be stimulated by insulin in a dose-dependent fashion and by IL-1 or tumor necrosis factor (Cobb and Rosen, 1983;Guy et al, 1991;Guesdon et al, 1993), and membraneassociated CKI activity can be inhibited by phosphatidylinositol 4,5-bisphosphate (Brockman and Anderson, 1991). Furthermore, sites phosphorylated by CKI both in vivo and in vitro have been determined for cAMP responsive element modulator (CREM) (de Groot et al, 1993), SV40 large T antigen (Cegielska and Virshup, 1993), glycogen synthase (Roach, 1991), and p53 (Milne et al, 1992). In CREM, the phosphorylation by CKI affects the DNA-binding activity of the transcription factor.…”

Section: Introductionmentioning

confidence: 99%

Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity.

Hoekstra

Dhillon

Carmel

et al. 1994

MBoC

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We have examined the activity and substrate specificity of the Saccharomyces cerevisiae Hrr25p and the Schizosaccharomyces pombe Hhpl, Hhp2, and Ckil protein kinase isoforms. These four gene products are isotypes of casein kinase I (CKI), and the sequence of these protein kinases predicts that they are protein serine/threonine kinases. However, each of these four protein kinases, when expressed in Escherichia coli in an active form, was recognized by anti-phosphotyrosine antibodies. Phosphoamino acid analysis of 32P-labeled proteins showed phosphorylation on serine, threonine, and tyrosine residues. The E. coli produced forms of Hhpl, Hhp2, and Ckil were autophosphorylated on tyrosine, and both Hhpl and Hhp2 were capable of phosphorylating the tyrosine-protein kinase synthetic peptide substrate polymer poly-E4Yl. Immune complex protein kinases assays from S. pombe cells showed that Hhpl-containing precipitates were associated with a protein-tyrosine kinase activity, and the Hhpl present in these immunoprecipitates was phosphorylated on tyrosine residues. Although dephosphorylation of Hhpl and Hhp2 by Ser/Thr phosphatase had little effect on the specific activity, tyrosine dephosphorylation of Hhpl and Hhp2 caused a 1.8-to 3.1-fold increase in the Km for poly-E4Y, and casein. These data demonstrate that four different CKI isoforms from two different yeasts are capable of protein-tyrosine kinase activity and encode dual-specificity protein kinases.

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“…The Stimulatory Effect of hC3a on CK-II Activity in Vitro Since hC3a is a basic protein, like HMG1 10,11) and human lactoferricin (hLFcin), 33) the stimulatory effect of hC3 on CK-II activity (phosphorylation of a-casein) was examined in vitro. CK-II was incubated with 5 mM [g-32 P]ATP (500 cpm/pmol) and a-casein in the presence of the indicated doses of hC3a or hLFcin as a CK-II activator in vitro.…”

Section: )mentioning

confidence: 99%

“…8,9) At least five isoforms (a, b, g, d and e) have been identified from a variety of cell sources. 8,9) It is well-known that these CK-I isoforms are implicated in a diverse number of cellular functions, including DNA replication, 10) DNA repair, 11) nuclear shuttling of transcriptional factors, 12) Wnt signaling, 13) and circadian rhythms. 14) However, the exact details of these CK-I-mediated regulatory mechanisms are unclear at present.…”

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confidence: 99%

The Effects of Cholesterol-3-sulfate (CH-3S) on the Phosphorylation of Human C3a (hC3a) <i>in Vitro</i> and on the Ability of hC3a to Induce Vascular Permeability in Rats

Kawakami

Ito

Matsuda

et al. 2004

Biological & Pharmaceutical Bulletin

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The phosphorylation of human C3a (hC3a, anaphylatoxin) by two distinct protein kinases (PKA and CK-I) and the effect of cholesterol-3-sulfate (CH-3S) on this phosphorylation were biochemically investigated in vitro. It was found that (i) hC3a functions as a phosphate acceptor for PKA and CK-I, but not for CK-II; (ii) the CK-Imediated phosphorylation of hC3a requires the presence of 3 m mM CH-3S in a manner similar to the phosphorylation of HMG1 (CH-3S-binding protein) by CK-I; and (iii) CH-3S inhibits the PKA-mediated phosphorylation of hC3a in a dose-dependent manner (ID 50 ‫؍‬approx. 2 m mM). As expected, hC3a containing high levels of Arg-and Lys-residues stimulated approx. 3-fold CK-II activity (phosphorylation of a a-casein) in vitro. However, no significant effect of hC3a on CK-II activity was observed when hC3a was preincubated with CH-3S or fully phosphorylated by PKA in vitro. Furthermore, preincubation of hC3a with CH-3S diminished the ability of hC3a to induce vascular permeability in rats. The results provided here suggest that (i) hC3a is a CH-3S-binding protein; and (ii) CH-3S functions as a potent inhibitor for its physiological activities, including phosphorylation by PKA and CK-I, in vitro.

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Control of simian virus 40 DNA replication by the HeLa cell nuclear kinase casein kinase I.

Cited by 64 publications

References 46 publications

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Identification, Cloning, and Mutational Analysis of the Casein Kinase 1 cDNA of the Malaria Parasite, Plasmodium falciparum

Budding and fission yeast casein kinase I isoforms have dual-specificity protein kinase activity.

The Effects of Cholesterol-3-sulfate (CH-3S) on the Phosphorylation of Human C3a (hC3a) <i>in Vitro</i> and on the Ability of hC3a to Induce Vascular Permeability in Rats

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