ライフサイエンスコーパス: CK2

1 tyrosine kinase activity of casein kinase 2 (CK2).

2 Western blotting to measure casein kinase 2 (CK2).

3 elevant signalling protein, casein kinase 2 (CK2).

4 including GPCR kinases and casein kinase 2 (CK2).

5 on of pERK, were unaffected by inhibition of CK2.

6 n1, as well as after NS5A phosphorylation by CK2.

7 otein complexes including the protein kinase CK2.

8 phorylation was confirmed using purified CK1/CK2.

9 horylated at serine 18 by the protein kinase CK2.

10 s system is also regulated by protein kinase CK2.

11 ICD) as a novel target of phosphorylation by CK2.

12 for association with MRE11 phosphorylated by CK2.

13 to Glu, SE) reduced Brg1 phosphorylation by CK2.

14 t on the crucial AIS protein, protein kinase CK2.

15 ing two Maf1 mutants (Maf1-id S388A and Maf1-ck2(0)) which lack all of the CK2 phosphosites implicate

16 f casein kinase 1 (CK1) and casein kinase 2 (CK2) (10 muM D4476, 100 muM CK2-inhibitory peptide YNLKS

17 CD5 activates casein kinase 2 (CK2), a serine/threonine kinase that constitutively asso

18 at Brg1 is also a target of casein kinase 2 (CK2), a serine/threonine kinase, in proliferating myobla

19 require the Cka2 subunit of casein kinase 2 (CK2), a ubiquitous enzyme with multiple cellular functio

20 Casein kinase II (formerly known as CK2), a ubiquitous Ser/Thr kinase, plays critical roles

21 Here we show that CK2, a ubiquitous and constitutively active protein kina

22 ing proteins to interact with protein kinase CK2: (a) the alpha and beta subunits of the nicotinic ac

23 omotion and exploration at baseline, whereas CK2 ablation in D2 receptor-positive neurons caused incr

24 indings prompted us to examine the impact of CK2 ablation on the effects of l-DOPA treatment in the u

25 physiological significance of CD5-dependent CK2 activation in T cells, we generated a knock-in mouse

26 M1 spastins on FAT involve casein kinase 2 (CK2) activation.

27 lpha2alpha3 triple mutants displayed reduced CK2 activity compared with wild-type seedlings.

28 In addition, CK2 activity controls the subcellular organization of in

29 In a number of animal tumors, CK2 activity has been shown to escape normal cellular co

30 n of Tyr 57 in H2A in yeast or inhibition of CK2 activity impairs transcriptional elongation in yeast

31 onfocal microscopy, here we demonstrate that CK2 activity is important for BTV replication.

32 CK2 activity is required for the interaction of FGF14 wi

33 These results link CK2 activity with SG disassembly.

34 Moreover, CK2 alpha subunit mutants are also hyposensitive to a Na

35 ination and cotyledon greening is reduced in CK2 alpha subunit mutants in an additive manner.

36 Taken together, these data suggest that CK2 alpha subunits affect diverse developmental and stre

37 CK2 alpha1alpha2alpha3 triple mutants also displayed red

38 Phenotypic characterization showed that CK2 alpha1alpha2alpha3 triple mutants are late flowering

39 The CK2 alpha1alpha2alpha3 triple mutants displayed reduced

40 riptional enhancer region of BIRC3; abundant ck2 also associated with this region in cells expressing

41 Phosphorylation of PRH by CK2 also decreases the nuclear association of PRH and in

42 he complexes at serine 424 by protein kinase CK2 (also known as casein kinase 2) activated the HDAC3

43 genetic ablation of the protein kinase CK2 (CK2) ameliorates experimental autoimmune encephalomyelit

44 ent actions of oxidative stress and elevated CK2 and ARF levels, which are common features of cancer

45 is controlled by the antagonistic action of CK2 and B56-containing PP2As, has an important impact on

46 Downregulation of CK2 and EGFR also caused deactivation of heat shock prot

47 ll lines LN229 and U87MG that expressed both CK2 and EGFR at different levels were used.

48 nobioconjugate that is directed against both CK2 and EGFR.

49 y in vitro seven bona fide sites modified by CK2 and GSK3beta kinases and two new sites on the PTEN C

50 te that two cascades of events controlled by CK2 and GSK3beta occur independently on two clusters of

51 RAS pathway proteins, including the kinases CK2 and p-ERK1/2 and the signaling scaffold KSR1.

52 e M-current, which is tonically regulated by CK2 and PP1 anchored to the KCNQ2 channel complex.

53 We also demonstrated that functional CK2 and protein phosphatase 1 (PP1) were selectively tet

54 ting subunit, as well as with protein kinase CK2 and protein phosphatase 2A, which modulate Ca(2+) se

55 f PRH on cell proliferation are abrogated by CK2 and that CK2 inhibits the binding of PRH at the Vegf

56 ce that Lac1 and Lag1 are direct targets for CK2 and that phosphorylation at conserved positions with

57 er regulator serine/threonine protein kinase CK2 and the wild-type/mutated epidermal growth factor re

58 ing epitopes of all four binding partners to CK2 and thereby gained insights into the potential role

59 ere secondary to PD-1-mediated inhibition of CK2 and were recapitulated by pharmacologic inhibition o

60 We focus on casein kinase 2 (CK2) and demonstrate that the regulatory (beta) and cata

61 eracting protein 1 (Dzip1), casein kinase 2 (CK2), and B56 containing protein phosphatase 2As (PP2As)

62 ctins as targets of the protein kinases CK1, CK2, and PKA.

63 ytosis, the kinase activities of MEK-ERK and CK2, and the presence of KSR1.

64 etochore protein Ndc10 are phosphorylated by CK2, and this phosphorylation plays antagonistic and syn

65 with FoxG1 to promote neuronal survival in a CK2- and PI3K-Akt-dependent manner.

66 onsistent with the previous observation that CK2 appears enriched at the NMJ.

67 ory (beta) and catalytic (alpha) subunits of CK2 are essential for synapse maintenance.

68 ts of mutant M1 spastin on FAT, and identify CK2 as a critical mediator of these effects.

69 Our results identify CK2 as a new target of PD-1 and reveal an unexpected mec

70 Thus, these results identify CK2 as a nodal point in TH17 cell development and sugges

71 Our data implicate CK2 as a regulator of the Th17/Treg axis and Th17 cell m

72 Together, our data identify CK2 as an important regulator of sphingolipid metabolism

73 Taken together, these findings identify CK2 as an upstream activating kinase of PAK1, providing

74 fect of enhanced 5-HT4 receptor activity and CK2 as modulator of 5-HT4 receptor levels in this brain

75 sly, we demonstrated that the protein kinase CK2 associates with and phosphorylates the receptor tyro

76 ion site at serine 124, and we now show that CK2 associates with Foxc2 and phosphorylates this site i

77 We demonstrate that CK2 associates with Mif2, the Saccharomyces cerevisiae h

78 confirmed direct phosphorylation of FGF14 by CK2 at S228 and S230, and mutation to alanine at these s

79 phosphorylation of TLE1 by casein kinase-2 (CK2) at Ser-239 and Ser-253 is necessary for its surviva

80 show that the 5-HT4 receptor is regulated by CK2, at transcriptional and post-transcriptional levels.

81 KCNQ3 anchor domains by protein kinase CK2 (CK2) augments binding, as previously shown for Nav1.2.

82 ery of at least four distinct kinases (PPKs, CK2, BIN2, and phytochrome itself) and four families of

83 nase that constitutively associates with the CK2-binding domain at the end of its cytoplasmic tail.

84 Casein kinase 2 (CK2) binds to the NHE3 C-terminus and constitutively pho

85 eals that CK2alpha, the catalytic subunit of CK2, binds across RNA-polymerase-II-transcribed coding g

86 ongly competes with Cl(-) uptake through CLC-ck2 but has no effect on CLC-ec1.

87 latelet-secreted kinases was enhanced, while CK2 but not CK1 inhibitors reduced APC cofactor activity

88 Inhibition of CK2 by siRNA or by pharmacological inhibitor restored No

89 Finally, inhibition of CK2 by TBBz or CK2 siRNA significantly enhances 1,25D(3)

90 the multitude of existing inhibitors against CK2, can serve as a structural basis for the design of n

91 sphorylation of calmodulin by protein kinase CK2 (casein kinase 2) rapidly and reversibly modulated K

92 al analyses demonstrated that protein kinase CK2-catalyzed phosphorylation of HDAC1 and -2 is crucial

93 on with selective inability to interact with CK2 (CD5DeltaCK2BD).

94 ll as genetic ablation of the protein kinase CK2 (CK2) ameliorates experimental autoimmune encephalom

95 2 and KCNQ3 anchor domains by protein kinase CK2 (CK2) augments binding, as previously shown for Nav1

96 orylated to nonphosphorylated protein kinase CK2 (CK2) substrate molecules, we employed (18)O-labeled

97 Biochemical studies demonstrate that the CK2 component of PRC1-AUTS2 neutralizes PRC1 repressive

98 These results suggest that CK2 contributes to 1,25D(3)-mediated target gene express

99 e that phosphorylation by the protein kinase CK2 controls the biochemical activities of the bovine pa

100 f translation regulation, whereby mTORC1 and CK2 coordinate TC and eIF4F complex assembly to stimulat

101 shment of PRH function through inhibition of CK2 could be of value in treatment of myeloid leukaemias

102 is and Th17 cell maturation and suggest that CK2 could be targeted for the treatment of Th17 cell-dri

103 we show that phosphorylation of PR Ser81 is ck2 dependent and progestin regulated in intact cells bu

104 Wnt stimulation induces the casein kinase 2 (CK2)-dependent phosphorylation of LRP6 at S1579, promoti

105 te PAK1 and that it is, rather, required for CK2-dependent PAK1(S223) phosphorylation that converts a

106 ies show that DUSP6 serves as a scaffold for ck2-dependent PR-B Ser81 phosphorylation and subsequent

107 detected in MKs and platelets, the impact of CK2-dependent signaling on MK/platelet (patho-)physiolog

108 ailed to undergo phosphorylation on Ser81, a ck2-dependent site required for expression of these gene

109 ation in transcriptional elongation based on CK2-dependent tyrosine phosphorylation of the globular d

110 We have also noted that casein kinase 2 (CK2)-directed phosphorylation of Pax7 attenuates caspase

111 We show that CK2 directly phosphorylates Dzip1 at four serine residue

112 Here we show that CK2 directly phosphorylates PIF1 at multiple sites.

113 on of a glutamate at the Glu(in) site in CLC-ck2 does not increase H(+) flux.

114 ive PACSIN 1 mutant, S358A, or inhibition of CK2 drastically reduces spine formation in neurons.

115 tive-feedback model in which a CRY-dependent CK2-driven posttranslational BMAL1-P-BMAL1 loop is an in

116 t phosphorylation of HDAC3 in the complex by CK2 during mitosis activates the complex for a dual role

117 recapitulated by pharmacologic inhibition of CK2 during TCR/CD3- and CD28-mediated stimulation withou

118 on XRCC1 phosphorylation by casein kinase 2 (CK2), enhancing XRCC1's interaction with the end resecti

119 In this article, we demonstrate that CK2 expression and kinase activity are induced upon CD4(

120 in DNA damage-resistant cytoplasmic PTEN and CK2 expression, and the attenuation of DNA repair genes.

121 In cultured mammalian cells, reducing CK2 expression, but not its kinase activity, decreases t

122 In turn, CK2 facilitated the binding of topoIIalpha to COP9 signa

123 These results suggest that a CK2-FGF14 axis may regulate Nav channels and neuronal ex

124 ed first by MEK and then by casein kinase 2 (CK2), followed by interaction with importin7 and subsequ

125 Together, this work reveals a novel CK2 function during the hyperosmotic stress response tha

126 polarization, but little is known about how CK2 functions in T cells.

127 We also showed that inhibition of CK2 greatly enhanced M3R-stimulated insulin secretion in

128 CK2 has enhanced expression or activity in numerous canc

129 cterial homolog from Citrobacter koseri, CLC-ck2, has yielded surprising discoveries about the requir

130 and additionally, because both ceramides and CK2 have been implicated in the regulation of cancer, ou

131 Several crystal structures of human CK2 have been published with different conformations for

132 s not detectably affect the stability of the CK2 holoenzyme but correlates with the reduced occupancy

133 minal residues of CK2alpha, is essential for CK2 holoenzyme complex stability and function in vivo.

134 The CK2 holoenzyme consists of two catalytic alpha subunits

135 value of 240nM and was shown to inhibit the CK2 holoenzyme-dependent phosphorylation of PDX-1, a sub

136 Ablation of CK2 in D1 receptor-positive striatal neurons caused enha

137 on are bidirectionally modulated by ablating CK2 in D1- or D2-positive projection neurons, in male an

138 his study, we revealed a regulatory role for CK2 in kinetochore function.

139 ent study, we demonstrate that inhibition of CK2 in pancreatic beta-cells, knockdown of CK2alpha expr

140 The role of CK2 in regulating MRP1 was confirmed in other cancer cel

141 The role of CK2 in regulation of NHE3 activity in polarized Caco-2/b

142 demonstrate a formerly undocumented role for CK2 in regulation of translation initiation, whereby CK2

143 ion of dyskinesia reveals a central role for CK2 in striatal physiology and indicates that both pathw

144 ression of LID, the kinase CK2: knock-out of CK2 in striatonigral and striatopallidal neurons has opp

145 We report here that knock-out of CK2 in striatonigral neurons reduces the severity of l-D

146 In contrast, lack of CK2 in striatopallidal neurons enhances LID and ERK phos

147 CK2 in turn phosphorylates TIF-IA, thereby increasing rD

148 To study the importance of CK2 in vivo, we have selectively knocked out CK2, in eit

149 e uncover a novel role for casein kinase II (CK2) in the cellular response to hyperosmotic stress.

150 ults highlighted a role for casein kinase 2 (CK2) in the modulation of dopamine D1 receptor (D1R) sig

151 , PTEN is phosphorylated by casein kinase 2 (CK2) in the Ser380-Thr382-Thr383 cluster within the C-te

152 as a specific site used by casein kinase 2 (CK2) in vitro and in vivo.

153 A single kinase, CK2, in D1-MSNs significantly alters dopamine signaling,

154 CK2 in vivo, we have selectively knocked out CK2, in either D1- or D2-medium spiny neurons (MSNs) and

155 CK2 inactivation results in developmental defects that p

156 Moreover, pharmacological inhibition of CK2 increased myoblast proliferation.

157 ever, phosphorylation of PS by CK2 or by CK1/CK2 increased PS cofactor activity approximately 1.5-fol

158 ted by elevated levels of the protein kinase CK2, increases topo I activity and the cellular sensitiv

159 Mechanistically, both CK2 inhibition and the H2A(Y57F) mutation enhance H2B de

160 s confirmed in other cancer cell lines where CK2 inhibition decreased MRP1-mediated efflux of doxorub

161 r pretreatment with calyculin A Furthermore, CK2 inhibition diminished the medium after hyperpolariza

162 Furthermore, CK2 inhibition or genetic ablation prevents TH17 cell de

163 CK2 inhibition restores PTEN nuclear distribution and DN

164 lles that are correctable by pharmacological CK2 inhibition.

165 ration of leukemia cells and synergizes with CK2 inhibition.

166 lation of CYP24A1 expression by 1,25D(3) and CK2 inhibitor enhances 1,25D(3)-mediated antitumor effec

167 sma membrane localization in the presence of CK2 inhibitor or shRNA targeting CK2alpha.

168 Treatment of wild-type MEFs with a CK2 inhibitor to block phosphorylation of the nuclear tr

169 CK2 inhibitor treatment suppressed M-current in rat supe

170 eatic islets with CX4945, a highly selective CK2 inhibitor, greatly reduced agonist-induced phosphory

171 nzotriazole (TBB), a potent casein kinase 2 (CK2) inhibitor, as a strong suppressor of FGF14:Nav1.6 i

172 Conversely, casein kinase-2 (CK2)-inhibitor increases Ikaros function thereby inhibit

173 They also suggest that CK2 inhibitors could release the full neuroprotective po

174 eno[1,2-b]indole-9,10-dione scaffold, potent CK2 inhibitors into selective ABCG2 inhibitors and vice

175 In the search for CK2 inhibitors, attention has expanded toward compounds

176 k inhibitors of CK2, whereas the most potent CK2 inhibitors, such as 4a, 4p, and 4e, displayed limite

177 were synthesized as human casein kinase II (CK2) inhibitors.

178 casein kinase 2 (CK2) (10 muM D4476, 100 muM CK2-inhibitory peptide YNLKSKSSEDIDESS).

179 proliferation are abrogated by CK2 and that CK2 inhibits the binding of PRH at the Vegfr-1 promoter.

180 oline-Rich Homeodomain protein (PRH/Hhex) by CK2 inhibits the DNA-binding activity of this transcript

181 PIAS1-mediated SUMOylation of PML promoted CK2 interaction and ubiquitin/proteasome-mediated degrad

182 CK2 interacts with and phosphorylates the Hot1 transcrip

183 We found that CK2 interacts with Brg1, and mutation of putative phosph

184 Here, we asked whether CK2 interacts with other proteins involved in processes

185 Second, and even more surprisingly, CLC-ck2 is a Cl(-)/H(+) antiporter, even though it contains

186 CK2 is a highly conserved and pleiotropic serine/threoni

187 Casein kinase CK2 is an essential enzyme in higher organisms, catalyzi

188 Endogenous CK2 is associated with JAK2 and JAK1 and phosphorylates

189 Increased activity of protein kinase CK2 is associated with various types of cancer, neurodeg

190 CK2 is considered to be a constitutively active kinase a

191 Whereas CK2 is dispensable for miRNA biogenesis and the stabilit

192 ary, our findings reveal that protein kinase CK2 is involved in the regulation of CYP24A1 expression

193 the differential occupancy of tRNA genes by CK2 is likely to modulate its activation of RNA polymera

194 ation is reinforced by the observations that CK2 is responsible for epidermal growth factor-induced P

195 Ion selectivity in CLC-ck2 is similar to that in CLC-ec1, except that SO(4)(2-)

196 CLC-ck2 is the first known antiporter that contains a nonpol

197 The protein kinase casein kinase 2 (CK2) is a pleiotropic and constitutively active kinase t

198 Although protein kinase casein kinase 2 (CK2) is readily detected in MKs and platelets, the impac

199 S2 dephosphorylation and that, together with CK2, it regulates VIB morphology and virus replication.

200 cka1a2a3 triple mutant has reduced levels of CK2 kinase activity and CIRCADIAN CLOCK ASSOCIATED1 phos

201 Inhibition of CK2 kinase by 2-dimethylamino-4,5,6,7-tetrabromo-1H-benz

202 player in the expression of LID, the kinase CK2: knock-out of CK2 in striatonigral and striatopallid

203 Furthermore, siRNA-mediated CK2 knockdown reduces 1,25D(3)-induced CYP24A1 mRNA expr

204 First, even though CLC-ck2 lacks conserved amino acids near the Cl(-)-binding s

205 Molecularly, inhibition of CK2 leads to reduced STAT3 phosphorylation and strongly

206 Remarkably, phosphorylated S164-SIRT1 and CK2 levels were also highly elevated in liver samples of

207 Proof-of-concept experiments using CK2-, MAPK- and EGFR-targeting assays in lung cancer cel

208 s, inhibition of phosphorylation of SIRT1 by CK2 may serve as a new therapeutic approach for treatmen

209 ious research suggests that casein kinase 2 (CK2) may be a promising therapeutic target for GBMs.

210 itro studies indicated that casein kinase 2 (CK2) mediated the phosphorylation of NS2, which regulate

211 n with p53 is modulated by casein kinase II (CK2)-mediated phosphorylation of a conserved acidic regi

212 Collectively, our findings suggest that CK2-mediated GluN2B phosphorylation contributes to incre

213 phorylation of beta-cell M3Rs, indicative of CK2-mediated M3R phosphorylation.

214 LRP6 receptor mutant (S1579A), deficient in CK2-mediated phosphorylation and Dab2 binding, fails to

215 tion of Mre11-S649 by Plk1 primed subsequent CK2-mediated phosphorylation at Mre11-serine 688 (S688).

216 Our results indicate that CK2-mediated phosphorylation of Brg1 regulates myoblast

217 These findings suggest that CK2-mediated phosphorylation of calmodulin regulates the

218 CK2-mediated phosphorylation of calmodulin strengthened

219 ning mutations at all seven sites eliminated CK2-mediated phosphorylation of PIF1 in vitro.

220 that interaction of ECD with RUVBL1, and its CK2-mediated phosphorylation, independent of its interac

221 altered activation of Hot1-targeted STL1 in ck2 mutants, resulting in a bimodal to unimodal shift in

222 have previously shown that casein kinase 2 (CK2) negatively regulates dopamine D1 and adenosine A2A

223 Inhibition of protein kinase CK2 normalized the GluN2B Ser(1480) phosphorylation leve

224 that increased activity of casein kinase 2 (CK2) observed in HPC and in MDSC could be responsible fo

225 rus (BPV) E2 protein, when phosphorylated by CK2 on two specific sites in the hinge, also loses its s

226 However, phosphorylation of PS by CK2 or by CK1/CK2 increased PS cofactor activity approxi

227 effects of chemical inhibition of Tyr kinase CK2 or by mutating the phosphorylation site.

228 Overexpression of CK2, particularly the alpha catalytic subunit (CK2alpha,

229 r recruitment, concurrently triggered by the CK2 phospho switch, provide an intriguing mechanism for

230 uppression was prevented by co-expression of CK2 phosphomimetic calmodulin mutants or pretreatment wi

231 CK2 phosphorylated 14-3-3gamma at serine residue 235 and

232 uggested that it is nuclear translocation of CK2-phosphorylated pERK that regulates cell proliferatio

233 The PNKP FHA domain binds to the CK2-phosphorylated XRCC4 C-terminal tail, while LigIV us

234 nd MRP1 interact physically, and recombinant CK2 phosphorylates MRP1-derived peptide in vitro in a Th

235 ur knowledge, the physiological relevance of CK2 phosphorylation of a GPCR and suggest the novel conc

236 atent viral DNA replication, indicating that CK2 phosphorylation of E2 is a negative regulator of vir

237 do not support the proposed requirement for CK2 phosphorylation of Maf1 during derepression of pol I

238 Recently it was proposed that CK2 phosphorylation of Maf1 is required for reactivation

239 CK2 phosphorylation of PACSIN 1 leads to a dissociation

240 perone family, whose actions are mediated by CK2 phosphorylation.

241 oes ubiquitin-mediated degradation primed by CK2 phosphorylation.

242 e and that their interaction is regulated by CK2 phosphorylation.

243 e polyanionic peptides typically produced by CK2 phosphorylation.

244 interaction is dependent on casein kinase 2 (CK2) phosphorylation of two acidic sequences within the

245 no terminus has a consensus casein kinase 2 (CK2) phosphorylation site at serine 124, and we now show

246 S388A and Maf1-ck2(0)) which lack all of the CK2 phosphosites implicated in the response.

247 CK2 physiologically phosphorylates IP6K2 at amino acid r

248 drial and nuclear proteins through consensus CK2, PKC phosphorylation, and N-myristoylation sites, an

249 While we know that CK2 plays a role(s) in cell division, our understanding

250 and casein kinase1 (CK1) and casein kinase2 (CK2) positively and negatively regulates CREB-mediated t

251 the external glutamate gate (Glu(ex)) in CLC-ck2 prevents H(+) flux.

252 Protein kinase CK2 promotes cell survival and the activity of this kina

253 n experiments, we show that casein kinase 2 (CK2) promotes stress granule dynamics.

254 d serine/threonine kinase, casein kinase II (CK2), promotes miRISC function in Caenorhabditis elegans

255 The CK2 protein itself is required to negatively regulate mR

256 lity as a consequence of aberrantly elevated CK2 provoked by p53 ablation and irrevocably deregulated

257 ined insights into the potential role of the CK2/Rapsyn interaction.

258 hat phospho-Ser81 PR provides a platform for ck2 recruitment and regulation of selected PR-B target g

259 it has been demonstrated that inhibitors of CK2 regressed tumor growth in GBM xenograft mouse models

260 ) in cell division, our understanding of how CK2 regulates cell cycle progression is limited.

261 The results reveal that CK2 regulates signaling events critical to LID in each o

262 The present study explored the impact of the CK2 regulatory beta-subunit on platelet biogenesis and a

263 to interact with microtubules in vitro, and CK2 reverses this inactivation (approximately fourfold)

264 abromobenzimidazole (TBBz), a protein kinase CK2 selective inhibitor as a disruptor of CYP24A1 promot

265 Accordingly, application of CK2-selective inhibitors suppressed KCNQ2 current.

266 These results demonstrate that CD5-CK2 signaling sets the threshold for T cell responsivene

267 We also found that functional CD5-dependent CK2 signaling was necessary for efficient differentiatio

268 Finally, inhibition of CK2 by TBBz or CK2 siRNA significantly enhances 1,25D(3)-mediated antip

269 Mass spectrometry revealed a phosphorylated CK2 site at Thr37 within the N-terminal Gla-domain.

270 ced through phosphorylation of the canonical CK2 site within the SIM.

271 550 of Dzip1, dephosphorylate Dzip1 on these CK2 sites.

272 expected potential secondary targets such as CK2, SLK, and the lipid kinase PIKfyve/Vac14/Fig4.

273 CS-3), a downstream target, are inhibited by CK2 small interfering RNAs or pharmacologic inhibitors.

274 of phospho-site mutation and treatment with CK2 specific inhibitors demonstrated that phosphorylatio

275 t mutation of S30 in BRMS1 or the use of the CK2-specific small-molecule inhibitor CX4945 abrogates C

276 egulation of translation initiation, whereby CK2 stimulates phosphorylation of eIF2beta and simultane

277 CK2 stimulates pol III transcription in yeast and human

278 DEAD-box RNA helicase, CGH-1/DDX6, as a key CK2 substrate within miRISC and demonstrate phosphorylat

279 ted to nonphosphorylated protein kinase CK2 (CK2) substrate molecules, we employed (18)O-labeled aden

280 opy-based assay that mimics the principle of CK2 subunit interaction by using CK2alpha1-335 and the f

281 Our studies demonstrate that the CK2 subunit, CK2alpha, is overexpressed in and has an im

282 However, the biological roles of CK2 subunits have not been fully characterized yet.

283 horylation was catalyzed by casein kinase 2 (CK2), the levels of which were dramatically elevated in

284 Inhibition of CK2 through TBB reduces the interaction of FGF14 with Na

285 tional complex consisting of PR-B, DUSP6 and ck2 to an enhancer region upstream of the Wnt1 promoter.

286 demonstrate that IP7, formed by IP6K2, binds CK2 to enhance its phosphorylation of the TTT complex, t

287 tify Ankyrin2 as a key presynaptic target of CK2 to maintain synapse stability.

288 parallel with phosphorylation of HP1/Swi6 by CK2 to restrict Epe1.

289 pharmacologic inhibition of casein kinase 2 (CK2) to eradicate disease in high-risk B-cell acute lymp

290 ated by the Cka2 subunit of casein kinase 2 (CK2) to promote its E3 activity for Cse4.

291 eport an apoptotic signaling cascade linking CK2, TTT, the PIKKs, and p53.

292 Thus, S223 is likely accessible to CK2 upon conformational changes of PAK1 induced by GTPas

293 Targeting the catalytic activity of CK2 using the next-generation small molecule inhibitor C

294 , and 4k, behaved as very weak inhibitors of CK2, whereas the most potent CK2 inhibitors, such as 4a,

295 BDNF signaling PACSIN 1 is phosphorylated by CK2 which is essential for spine formation.

296 lance to that of eukaryotic casein kinase 2 (CK2), which also exhibits dual nucleotide specificity.

297 Increased levels of casein kinase (CK1 and CK2), which are associated with TDP-43 phosphorylation,

298 on at threonine 13 (T13) by casein kinase 2 (CK2), which in turn triggers direct binding to the Nijme

299 threonine 205 (Thr205), a consensus site for CK2, which appears to play a key regulatory role in modu

300 kinase Kns1, may regulate the association of CK2 with some of its substrates by phosphorylating Ckb1.