scholarly journals The casein kinase 2 β subunit CK2B1 is required for swollen stem formation via cell cycle control in vegetable Brassica juncea

2020 ◽  
Vol 104 (3) ◽  
pp. 706-717
Author(s):  
Lili Zhang ◽  
Zhangping Li ◽  
Jenella Garraway ◽  
Qingze Cai ◽  
Yufeng Zhou ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Brassica Juncea ◽  
Cell Cycle Control ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Β Subunit ◽  
Vegetable Brassica

Novel Anthraquinone Derivatives as Dual Inhibitors of Topoisomerase 2 and Casein Kinase 2: In Silico Studies, Synthesis and Biological Evaluation on Leukemic Cell Lines

2019 ◽  
Vol 18 (11) ◽  
pp. 1551-1562 ◽  
Author(s):  
Abbas Kabir ◽  
Kalpana Tilekar ◽  
Neha Upadhyay ◽  
C.S. Ramaa
Keyword(s):  
Cell Cycle ◽  
Cell Line ◽  
Cell Lines ◽  
Biological Evaluation ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Cell Cycle Analysis ◽  
Protein Targets ◽  
Topoisomerase 2 ◽  
Dual Inhibitors

Background: Cancer being a complex disease, single targeting agents remain unsuccessful. This calls for “multiple targeting”, wherein a single drug is so designed that it will modulate the activity of multiple protein targets. Topoisomerase 2 (Top2) helps in removing DNA tangles and super-coiling during cellular replication, Casein Kinase 2 (CK2) is involved in the phosphorylation of a multitude of protein targets. Thus, in the present work, we have tried to develop dual inhibitors of Top2 and CK2. Objective: With this view, in the present work, 2 human proteins, Top2 and CK2 have been targeted to achieve the anti-proliferative effects. Methods: Novel 1-acetylamidoanthraquinone (3a-3y) derivatives were designed, synthesized and their structures were elucidated by analytical and spectral characterization techniques (FTIR, 1H NMR, 13C NMR and Mass Spectroscopy). The synthesized compounds were then subjected to evaluation of cytotoxic potential by the Sulforhodamine B (SRB) protein assay, using HL60 and K562 cell lines. Ten compounds were analyzed for Top2, CK2 enzyme inhibitory potential. Further, top three compounds were subjected to cell cycle analysis. Results: The compounds 3a to 3c, 3e, 3f, 3i to 3p, 3t and 3x showed excellent cytotoxic activity to HL-60 cell line indicating their high anti-proliferative potential in AML. The compounds 3a to 3c, 3e, 3f, 3i to 3p and 3y have shown good to moderate activity on K-562 cell line. Compounds 3e, 3f, 3i, 3x and 3y were found more cytotoxic than standard doxorubicin. In cell cycle analysis, the cells (79-85%) were found to arrest in the G0/G1 phase. Conclusion: We have successfully designed, synthesized, purified and structurally characterized 1- acetylamidoanthraquinone derivatives. Even though our compounds need design optimization to further increase enzyme inhibition, their overall anti-proliferative effects were found to be encouraging.

scholarly journals Phosphorylation by Casein Kinase 2 Regulates Nap1 Localization and Function

2007 ◽  
Vol 28 (4) ◽  
pp. 1313-1325 ◽  
Author(s):  
Meredith E. K. Calvert ◽  
Kristin M. Keck ◽  
Celeste Ptak ◽  
Jeffrey Shabanowitz ◽  
Donald F. Hunt ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
S Phase ◽  
Bud Formation ◽  
Evolutionarily Conserved ◽  
Assembly Factor ◽  
And Function ◽  
Cycle Regulation

ABSTRACT In Saccharomyces cerevisiae, the evolutionarily conserved nucleocytoplasmic shuttling protein Nap1 is a cofactor for the import of histones H2A and H2B, a chromatin assembly factor and a mitotic factor involved in regulation of bud formation. To understand the mechanism by which Nap1 function is regulated, Nap1-interacting factors were isolated and identified by mass spectrometry. We identified several kinases among these proteins, including casein kinase 2 (CK2), and a new bud neck-associated protein, Nba1. Consistent with our identification of the Nap1-interacting kinases, we showed that Nap1 is phosphorylated in vivo at 11 sites and that Nap1 is phosphorylated by CK2 at three substrate serines. Phosphorylation of these serines was not necessary for normal bud formation, but mutation of these serines to either alanine or aspartic acid resulted in cell cycle changes, including a prolonged S phase, suggesting that reversible phosphorylation by CK2 is important for cell cycle regulation. Nap1 can shuttle between the nucleus and cytoplasm, and we also showed that CK2 phosphorylation promotes the import of Nap1 into the nucleus. In conclusion, our data show that Nap1 phosphorylation by CK2 appears to regulate Nap1 localization and is required for normal progression through S phase.

scholarly journals Expression of the Casein Kinase 2 Subunits in Chinese Hamster Ovary and 3T3 L1 Cells Provides Information on the Role of the Enzyme in Cell Proliferation and the Cell Cycle

1999 ◽  
Vol 274 (46) ◽  
pp. 32988-32996 ◽  
Author(s):  
Dongxia Li ◽  
Grazyna Dobrowolska ◽  
Lauri D. Aicher ◽  
Mingzi Chen ◽  
Jocelyn H. Wright ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Proliferation ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster ◽  
Casein Kinase ◽  
Casein Kinase 2

scholarly journals Casein Kinase 2 β-Subunit Is a Regulator of Bone Morphogenetic Protein 2 Signaling

2010 ◽  
Vol 99 (3) ◽  
pp. 897-904 ◽  
Author(s):  
Beth Bragdon ◽  
Shayamala Thinakaran ◽  
Oleksandra Moseychuk ◽  
Daniel King ◽  
Kira Young ◽  
...  
Keyword(s):  
Bone Morphogenetic Protein ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Bone Morphogenetic Protein 2 ◽  
Β Subunit ◽  
Morphogenetic Protein

Casein kinase-2 phosphorylates serine-2 in the β-subunit of initiation factor-2

1989 ◽  
Vol 1010 (3) ◽  
pp. 377-380 ◽  
Author(s):  
Stephanie J. Clark ◽  
Anthony J. Ashford ◽  
Nigel T. Price ◽  
Christopher G. Proud
Keyword(s):  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Initiation Factor ◽  
Β Subunit ◽  
Initiation Factor 2
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