Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of cis-diaminedichloroplatinum(II) (cisplatin) on the induction of p53 and protein kinase CK2 activity was studied in the mouse teratocarcinoma cell line F9. Treatment of the cells with the chemotherapeutic agent cisplatin led to the detection of p53 3 h after addition of the drug. F9 cell extracts treated with and without cisplatin were analyzed by ion exchange chromatography for protein kinase CK2 alpha/beta subunits and p53 distribution. The following results were obtained: (a) in crude extracts of cisplatin-treated cells, CK2 activity was sometimes reduced by as much as 50%; (b) after separation by anionic exchange chromatography (MA7Q, BioRad) of the crude cellular extracts from cisplatin-treated cells, lower CK2 activity was found in the peak fractions confirming the results obtained with crude cellular extracts; (c) besides the detection of CK2 alpha subunit by immunostaining, we have detected, at a concentration of approximately 200 mM NaCl, a protein of approximately 46 kDa which reacted with the CK2 alpha-specific antibody. This fraction was devoid of CK2 activity; and (d) cisplatin-treated cells exhibited p53 protein, which was mostly eluting ahead but also partly together with CK2 holoenzyme.
Cell Mol Biol Res 1994
PMID:Characterization of protein kinase CK2 protein subunits and p53 in F9 teratocarcinoma cells in the absence and presence of cisplatin. 773 33

The Drosophila serendipity (sry) beta and delta genes, which resulted from a gene duplication event, provide an interesting model for the evolutionary diversification in structure and function of C2H2 zinc finger proteins. We examined here the divergence of the sry beta and delta proteins over an estimated period of 45 million years by comparing their predicted sequences in D. melanogaster, D. pseudoobscura, and D. subobscura. Between orthologs, i.e., pairs of either sry beta or sry delta, the NH2-proximal region delineated by pairs of C-X2-C motifs and the DNA-binding finger domain are highly conserved. Sequence conservation operates over the entire finger domain, including the links separating adjacent fingers, even though each has a unique sequence different from the widespread TGEKP motif. In contrast, the sequence of the central acidic region has extensively diverged and differs between species in the number of amino acids, probably because of slippage-driven mutations. The NH2-terminal region and fingers 1, 5, and 6 differentiate the sry beta and delta proteins while zinc fingers 2, 3, and 4 are virtually identical in these two paralogs. A nuclear localization signal of the SV40T antigen type, preceded by a potential CKII phosphorylation regulatory site, is conserved in sry delta but not found in sry beta. The interspecific conserved regions correlate well with the positions of zygotic lethal mutations in the D. melanogaster sry delta protein. Furthermore, P-element transformation experiments show that a transgenic copy of the D. pseudoobscura sry delta gene rescues the sry delta mutant phenotype. Convergence of genetic and structural data on the sry proteins supports a multimodular function and mode of evolution of these C2H2 finger proteins.
J Mol Evol 1994 Mar
PMID:Interspecific comparison of Drosophila serendipity delta and beta: multimodular structure of these C2H2 zinc finger proteins. 800 93

Spermine-stimulated and heparin-inhibited phosphorylation of both exogenous casein and endogenous protein substrates of the prothoracic gland were measured in prothoracic gland cytosolic fractions from fifth instar larvae and early pupae of the tobacco hornworm, Manduca sexta. The results reveal a striking increase in casein kinase II (CKII) activity, i.e. approximately 3-fold above basal level in the presence of 5 mM spermine, with the highest activity exhibited by gland fractions from day 0-2 larvae, newly pupated animals and day 1 pupae. These results were verified by the results from Western blot analysis using a CKII alpha-subunit specific antibody and a 10 a.a. synthetic peptide that is a specific substrate for CKII. Several endogenous proteins were found to be substrates for CKII when assayed in the presence of spermine or polylysine. A 19 kDa peptide was shown to be calmodulin (CaM) by using the purified Manduca brain CaM as an indicator, and was only phosphorylated in the presence of polylysine. A 52 kDa protein was identified as tubulin by immunoprecipitation with a tubulin-specific monoclonal antibody, and was shown to be phosphorylated in the presence of spermine and polylysine. The possible roles of phosphocalmodulin and phosphotubulin are discussed in the context of prothoracic gland function.
Mol Cell Endocrinol 1994 Feb
PMID:Spermine and polylysine enhanced phosphorylation of calmodulin and tubulin in an insect endocrine gland. 818 51

A true protein kinase CKII (CKII) activity was characterized in liver mitochondria by its phosphorylating activity on the specific peptide substrate of CKII, the binding and elution profile of the enzyme on a phosphocellulose column and immunostaining of a 36 kDa polypeptide with antibodies against the alpha-subunit of human CKII. This CKII activity was located predominantly in the intermembrane space of quiescent mitochondria. A translocation of the enzyme to inner membrane of energized mitochondria occurred in the presence of spermine. Translocated CKII activity was tightly bound to inner membrane, and high salt concentrations were necessary to release the activity. The inner face of the inner membrane could constitute the in vivo localization of mitochondrial CKII since the potential substrates of the enzyme are 4 matrix proteins.
Cell Mol Biol (Noisy-le-grand) 1996 Mar
PMID:Evidence of true protein kinase CKII activity in mitochondria and its spermine-mediated translocation to inner membrane. 869 55

We examined the androgenic regulation of protein kinase CK1 in rat ventral prostate cytosolic and chromatin fractions. On androgen deprivation, CK1 in both the nuclear and cytoplasmic compartments decreases slowly at a similar rate. Stimulation of regrowth in the prostate does not evoke an early differential modulation in the CK1 because it increased in both the cytosol and chromatin only by 24 h after androgenic stimulus. These changes in CK1 relate to its proposed role in cell regulation at mitosis and differ from those in protein kinase CK2 that demonstrates rapid modulations in the nuclear compartment under similar conditions.
Cell Mol Biol Res 1995
PMID:Androgenic regulation of protein kinase CK1 in the prostatic cell. 886 89

Mos is a germ cell-specific serine/threonine kinase and is required for Xenopus oocyte maturation. Active Mos stimulates a mitogen-activated protein kinase (MAPK) by directly phosphorylating and activating MAPK kinase (MKK). We report here that the Xenopus homolog of the beta subunit of casein kinase II (CKII beta) binds to and regulates Mos. The Mos-interacting region of CKII beta was mapped to the C terminus. Mos bound to CKII beta in somatic cells ectopically expressing Mos and CKII beta as well as in unfertilized Xenopus eggs. CKII beta inhibited Mos-mediated MAPK activation in rabbit reticulocyte lysates and repressed MKK activation by v-Mos in a coupled kinase assay. In addition, microinjection of CKII beta mRNA into Xenopus oocytes inhibited progesterone-induced meiotic maturation and MAPK activation, presumably by binding of CKII beta to Mos and thereby inhibiting MAPK activation. Moreover, this inhibitory phenotype could be rescued by another protein that binds to CKII beta, CKII alpha. The ability of ectopic CKII beta to inhibit meiotic maturation and the detection of a complex between endogenous Mos and CKII beta suggest that CKII beta may act as an inhibitor of Mos during oocyte maturation, perhaps setting a threshold beyond which Mos protein must accumulate before it can activate the MAPK pathway.
Mol Cell Biol 1997 Apr
PMID:The casein kinase II beta subunit binds to Mos and inhibits Mos activity. 912 38

Casein kinase II from the yeast Yarrowia lipolytica is a heterotetramer of the form alpha alpha' beta 2. We report on the cloning and sequencing of a partial cDNA and of the complete genomic DNA coding for the catalytic alpha subunit of the casein kinase II from this yeast species. The sequence of the gene coding for this enzyme has been analyzed. No intron was found in the gene, which is present in a single copy. The deduced amino acid sequence of the gene shows high similarity with those of alpha subunit described in other species, although, uniquely, Y. lipolytica CKII alpha lacks cysteines. We find that the alpha subunit sequence of Y. lipolytica CKII is shown greater homology with the corresponding protein from S. pombe than with that from S. cerevisiae. We have analyzed CKII alpha expression and CKII alpha activity. We show that expression of this enzyme is regulated. The catalytic subunit is translated from a single mRNA, and the enzyme is present at a very low level in Y. lipolytica, as in other yeasts.
Mol Gen Genet 1997 Oct
PMID:Cloning of the gene encoding the catalytic subunit of casein kinase II from the yeast Yarrowia lipolytica. 939 33

A major pathway for K+ efflux in human reticulocytes and young RBCs is K:Cl cotransport (K:Cl-CT). The activity of K:Cl-CT is increased in pathologic RBCs containing hemoglobins S and C and may contribute to the abnormal dehydration state of these cells. Human K:Cl-CT (gene product KCC1) has been recently sequenced from human (hKCC1), rabbit and rat tissue by Gillen et al. (J Biol Chem 271:16237, 1996). We report here the sequence of KCC1 from human and mouse erythroleukemic cells (K562 and MEL cells, respectively). The cDNA for human erythroid-KCC1 is 100% identical to hKCC1 and the cDNA for mouse erythroid-KCC1 shares 89% identity with hKCC1, which translates to 96% identity at the amino acid level. Mammalian KCC1 is strongly conserved with >95% identity between human, rabbit, rat, and mouse KCC1 proteins. We did not detect any full-length mRNA transcripts of human erythroid-KCC1 in circulating reticulocytes. We detected two mRNA isoforms of human erythroid-KCC1 that resulted in C-terminal truncated proteins (73 amino acid and 17 amino acids, respectively). Human and mouse erythroidKCC1 differed at several consensus sites including a predicted PKC phosphorylation site at 108threonine and a predicted CK2 phosphorylation site at 51serine, within the predicted cytoplasmic N-terminal, that are present in human but not mouse erythroid-KCC1. Expression of MEL-KCC1 mRNA increases substantially upon DMSO-induced differentiation opening the possibility that erythroid-KCC1 plays a role in early erythroid maturation events. The molecular identification of erythroid-KCC1 is an important step towards understanding the physiologic role mediated by this protein in young and pathologic RBCs and during erythropoiesis, as well as providing a new tool for the elucidation of pathways and signals involved in RBC volume regulation.
Blood Cells Mol Dis 1998 Mar
PMID:Molecular identification and expression of erythroid K:Cl cotransporter in human and mouse erythroleukemic cells. 951 79

E. Coli RNA polymerase was phosphorylated with protein kinase CKII and allowed to bind to pBR322. After digestion of the RNA polymerase-pBR322 complex with proteinase K, the phosphopeptides that remained bound to DNA were extracted and analyzed. These phosphopeptides are able to bind again to DNA and to inhibit transcription.
Mol Cell Biochem 1998 Jan
PMID:Phosphopeptides derived from in vitro phosphorylated E. coli RNA polymerase bind to DNA and affect DNA transcription. 954 25

Protein kinase CKII (CKII) is a ubiquitous protein serine/threonine kinase. CKII usually exists in tetrameric complexes composed of two catalytic (CKII alpha and/or CKII alpha') and two regulatory (CKII beta) subunits. In the present study, using a combined in vivo and in vitro approach, we have investigated the role of CKII subunits in the formation of the tetrameric structure of CKII and the formation of the polymeric structure of CKII holoenzyme. Our in vivo experiments show that CKII beta interacts with either another CKII beta or CKII alpha and that CKII alpha does not interact with another CKII alpha (or CKII alpha'). Our in vitro experiments also show that CKII beta is able to associate with both CKII alpha and another CKII beta and that CKII alpha exists as a monomeric form in solution. These data indicate that CKII beta mediates the formation of a tetramer by both the dimerization of CKII beta and the interaction of CKII beta with CKII alpha. The results of this study also suggest that CKII beta may be involved in the formation of the polymeric structure of the CKII holoenzyme.
Mol Cells 1998 Feb 28
PMID:Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro. 957 30


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