Nuclear localization of protein kinase CK2 catalytic subunit (CK2α) is associated with poor prognostic factors in human prostate cancer

2007 ◽  
Vol 43 (5) ◽  
pp. 928-934 ◽  
Author(s):  
Mathieu Laramas ◽  
Dominique Pasquier ◽  
Odile Filhol ◽  
François Ringeisen ◽  
Jean-Luc Descotes ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Prognostic Factors ◽  
Protein Kinase ◽  
Nuclear Localization ◽  
Protein Kinase Ck2 ◽  
Catalytic Subunit ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Kinase Ck2

scholarly journals Activation of protein kinase CK2 attenuates FOXO3a functioning in a PML-dependent manner: implications in human prostate cancer

2013 ◽  
Vol 4 (3) ◽  
pp. e543-e543 ◽  
Author(s):  
A Chatterjee ◽  
U Chatterjee ◽  
M K Ghosh
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase ◽  
Protein Kinase Ck2 ◽  
Human Prostate ◽  
Dependent Manner ◽  
Human Prostate Cancer ◽  
Kinase Ck2

scholarly journals Inhibition of Protein Kinase CK2 Reduces Cyp24a1 Expression and Enhances 1,25-Dihydroxyvitamin D3 Antitumor Activity in Human Prostate Cancer Cells

2013 ◽  
Vol 73 (7) ◽  
pp. 2289-2297 ◽  
Author(s):  
Wei Luo ◽  
Wei-Dong Yu ◽  
Yingyu Ma ◽  
Mikhail Chernov ◽  
Donald L. Trump ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase ◽  
Antitumor Activity ◽  
Cancer Cells ◽  
Protein Kinase Ck2 ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Prostate Cancer Cells ◽  
Dihydroxyvitamin D3 ◽  
Kinase Ck2

scholarly journals The catalytic subunit of protein kinase CK2 phosphorylates in vitro the movement protein of Tomato mosaic virus

2003 ◽  
Vol 84 (2) ◽  
pp. 497-505 ◽  
Author(s):  
Yasuhiko Matsushita ◽  
Mayumi Ohshima ◽  
Kuniaki Yoshioka ◽  
Masamichi Nishiguchi ◽  
Hiroshi Nyunoya
Keyword(s):  
Protein Kinase ◽  
Mosaic Virus ◽  
Protein Kinase Ck2 ◽  
Movement Protein ◽  
Catalytic Subunit ◽  
Tomato Mosaic Virus ◽  
Kinase Ck2

Novel properties of the protein kinase CK2-site-regulated nuclear- localization sequence of the interferon-induced nuclear factor IFI 16

2000 ◽  
Vol 353 (1) ◽  
pp. 69-77 ◽  
Author(s):  
Lyndall J. BRIGGS ◽  
Ricky W. JOHNSTONE ◽  
Rachel M. ELLIOT ◽  
Chong-Yun XIAO ◽  
Michelle DAWSON ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Protein Kinase Ck2 ◽  
Protein Import ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Nuclear Localization Sequence ◽  
Localization Sequence ◽  
Kinase Ck2

Members of the interferon-induced class of nuclear factors possess a putative CcN motif, comparable with that within proteins such as the simian virus 40 large tumour antigen (T-ag), which confers phosphorylation-mediated regulation of nuclear-localization sequence (NLS)-dependent nuclear import. Here we examine the functionality of the interferon-induced factor 16 (IFI 16) CcN motif, demonstrating its ability to target a heterologous protein to the nucleus, and to be phosphorylated specifically by the CcN-motif-phosphorylating protein kinase CK2 (CK2). The IFI 16 NLS, however, has novel properties, conferring ATP-dependent nuclear import completely independent of cytosolic factors, as well as binding to nuclear components. The IFI 16 NLS is not recognized with high affinity by the NLS-binding importin heterodimer, and transport mediated by it is insensitive to non-hydrolysable GTP analogues. The IFI 16 NLS thus mediates nuclear import through a pathway completely distinct from that of conventional NLSs, such as that of T-ag, but intriguingly resembling that of the NLS of the HIV-1 transactivator protein Tat. Since the IFI 16 CK2 site enhances nuclear import through facilitating binding to nuclear components, this represents a novel mechanism by which the site regulates nuclear-protein import, and constitutes a difference between the IFI 16 and Tat NLSs that may be of importance in the immune response.

High-level expression of fatty acid synthase in human prostate cancer tissues is linked to activation and nuclear localization of Akt/PKB

2005 ◽  
Vol 206 (2) ◽  
pp. 214-219 ◽  
Author(s):  
Tine Van de Sande ◽  
Tania Roskams ◽  
Evelyne Lerut ◽  
Steven Joniau ◽  
Hein Van Poppel ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Fatty Acid ◽  
Nuclear Localization ◽  
Fatty Acid Synthase ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
High Level Expression ◽  
High Level ◽  
Cancer Tissues

scholarly journals Live-Cell Fluorescence Imaging Reveals the Dynamics of Protein Kinase CK2 Individual Subunits

2003 ◽  
Vol 23 (3) ◽  
pp. 975-987 ◽  
Author(s):  
Odile Filhol ◽  
Arsenio Nueda ◽  
Véronique Martel ◽  
Delphine Gerber-Scokaert ◽  
Maria José Benitez ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nuclear Localization ◽  
Protein Kinase Ck2 ◽  
Fluorescent Protein ◽  
Nuclear Translocation ◽  
Nuclear Accumulation ◽  
Nucleocytoplasmic Trafficking ◽  
Green Fluorescent ◽  
Nucleocytoplasmic Distribution ◽  
Kinase Ck2

ABSTRACT Protein kinase CK2 is a multifunctional enzyme which has long been described as a stable heterotetrameric complex resulting from the association of two catalytic (α or α′) and two regulatory (β) subunits. To track the spatiotemporal dynamics of CK2 in living cells, we fused its catalytic α and regulatory β subunits with green fluorescent protein (GFP). Both CK2 subunits contain nuclear localization domains that target them independently to the nucleus. Imaging of stable cell lines expressing low levels of GFP-CK2α or GFP-CK2β revealed the existence of CK2 subunit subpopulations exhibiting differential dynamics. Once in the nucleus, they diffuse randomly at different rates. Unlike CK2β, CK2α can shuttle, showing the dynamic nature of the nucleocytoplasmic trafficking of the kinase. When microinjected in the cytoplasm, the isolated CK2 subunits are rapidly translocated into the nucleus, whereas the holoenzyme complex remains in this cell compartment, suggesting an intramolecular masking of the nuclear localization sequences that suppresses nuclear accumulation. However, binding of FGF-2 to the holoenzyme triggers its nuclear translocation. Since the substrate specificity of CK2α is dramatically changed by its association with CK2β, the control of the nucleocytoplasmic distribution of each subunit may represent a unique potential regulatory mechanism for CK2 activity.

scholarly journals Protein kinase CK2 impact on intracellular calcium homeostasis in prostate cancer

2020 ◽  
Vol 470 (1-2) ◽  
pp. 131-143
Author(s):  
Muhammad Afzal ◽  
Betsy T. Kren ◽  
A. Khaliq Naveed ◽  
Janeen H. Trembley ◽  
Khalil Ahmed
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase ◽  
Intracellular Calcium ◽  
Calcium Homeostasis ◽  
Protein Kinase Ck2 ◽  
Intracellular Calcium Homeostasis ◽  
Kinase Ck2

scholarly journals Protein kinase Cɛ interacts with Bax and promotes survival of human prostate cancer cells

Oncogene ◽  
2003 ◽  
Vol 22 (39) ◽  
pp. 7958-7968 ◽  
Author(s):  
Meagan A McJilton ◽  
C Van Sikes ◽  
Ginger G Wescott ◽  
Daqing Wu ◽  
Tonia L Foreman ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Prostate Cancer Cells
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