Casein Kinase 2 Down-Regulation and Activation by Polybasic Peptides Are Mediated by Acidic Residues in the 55-64 Region of the .beta.-Subunit. A Study with Calmodulin As Phosphorylatable Substrate

Biochemistry ◽  
1994 ◽  
Vol 33 (14) ◽  
pp. 4336-4342 ◽  
Author(s):  
Flavio Meggio ◽  
Brigitte Boldyreff ◽  
Olaf-Georg Issinger ◽  
Lorenzo A. Pinna
Keyword(s):  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Beta Subunit ◽  
Down Regulation ◽  
Subunit A ◽  
Acidic Residues

scholarly journals Molecular cloning and mapping of casein kinase 2 alpha and beta subunit genes in barley

Genome ◽  
2008 ◽  
Vol 51 (3) ◽  
pp. 208-215 ◽  
Author(s):  
K. Kato ◽  
S. Kidou ◽  
H. Miura
Keyword(s):  
Single Copy ◽  
Hybridization Experiment ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Beta Subunit ◽  
Cdna Clones ◽  
Cdna Sequences ◽  
Chromosome Assignment ◽  
Chromosome Addition ◽  
Chromosome Addition Lines

Casein kinase 2 (CK2) is a ubiquitous, highly pleiotropic, constitutively active, and messenger-independent Ser/Thr protein kinase. It is found in two different forms: the heterotetrameric CK2, composed of two alpha catalytic subunits and two beta regulatory subunits, and the monomeric CK2 alpha, consisting of the alpha catalytic subunit. In the present study, we isolated barley cDNA clones of the CK2 alpha and beta subunit genes, designated HvCK2A and HvCK2B, respectively. Chromosome assignment, using a set of wheat–barley disomic chromosome addition lines, and RFLP mapping, using two doubled haploid populations, showed that HvCK2A was duplicated on the short arm of chromosome 2H and the long arm of chromosome 5H (designated HvCK2a-2H and HvCK2a-5H, respectively), and a single copy of HvCK2B was located on the long arm of chromosome 1H (designated HvCK2b). A PCR-Southern hybridization experiment demonstrated that the HvCK2A sequence originated from the HvCK2a-5H locus, showing that at least HvCK2a-5H was expressed. The present cDNA sequences and genomic organization of the two subunits will facilitate further functional analysis of CK2 in barley.

scholarly journals Heterogeneity of rat liver cytosol casein kinase 2. Association between the α/α' -subunits of casein kinase 2 and the phosphorylatable protein pp49

1991 ◽  
Vol 277 (3) ◽  
pp. 811-818 ◽  
Author(s):  
E Molina ◽  
M Plana ◽  
E Itarte
Keyword(s):  
Rat Liver ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Beta Subunit ◽  
Kinetic Properties ◽  
Liver Cytosol ◽  
Alpha Subunits ◽  
Beta Casein ◽  
Casein Kinases ◽  
Rat Liver Cytosol

Casein kinase 2 activity could be resolved into three peaks by chromatography on DEAE-Sepharose. The peak eluted at high salt concentrations (casein kinase 2b) showed molecular and kinetic properties typical of the heterotetramer composed of alpha-(or alpha'-) and beta-subunits. In contrast, the peak that was eluted at low salt concentrations (casein kinase 2a) contained no beta-subunit but a phosphorylatable protein of 49 kDa (pp49), in addition to the alpha/alpha'-subunits. The presence of alpha/alpha'/alpha"-subunits in preparations of casein kinases 2a and 2b was confirmed by immunological assays. Casein kinase 2a had low specific activity and a very high apparent Km for beta-casein. The peak eluted at intermediate ionic strength contained the alpha/alpha'-subunits and variable amounts of beta-subunit and pp49, and had kinetic properties intermediate between those of casein kinases 2a and 2b. Experiments based on heat inactivation, inhibition by low concentrations of heparin and ability to use GTP as substrate suggested that phosphorylation of pp49 was catalysed by the alpha/alpha'-subunits of casein kinase 2. No similarities were observed in the phosphopeptide maps of pp49 and beta-subunit. These results show that the alpha/alpha'-subunits of rat liver cytosol casein kinase 2 can form complexes not only with the beta-subunit but also with pp49, and that the complexes containing pp49 have a reduced affinity for the exogenous protein substrate beta-casein.

scholarly journals The beta subunit of casein kinase 2 as a novel binding partner of the ribosomal protein S6 kinase 1

2005 ◽  
Vol 21 (5) ◽  
pp. 407-412 ◽  
Author(s):  
G. G. Panasyuk ◽  
I. O. Nemzanyy ◽  
A. M. Zhyvoloup ◽  
V. V. Filonenko ◽  
I. T. Gout
Keyword(s):  
Ribosomal Protein ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Beta Subunit ◽  
S6 Kinase ◽  
Binding Partner ◽  
Ribosomal Protein S6 ◽  
Ribosomal Protein S6 Kinase

scholarly journals Role of the beta subunit of casein kinase-2 on the stability and specificity of the recombinant reconstituted holoenzyme

1992 ◽  
Vol 204 (1) ◽  
pp. 293-297 ◽  
Author(s):  
Flavio MEGGIO ◽  
Brigitte BOLDYREFF ◽  
Oriano MARIN ◽  
Lorenzo A. PINNA ◽  
Olaf-Georg ISSINGER
Keyword(s):  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Beta Subunit ◽  
The Stability

Statins as the Controlling Agents for Non-Hodgkin's Lymphomas via Increasing the Casein Kinase 2 Interacting Protein-1: A Hypothesis

2020 ◽  
Vol 17 (5) ◽  
pp. 616-618
Author(s):  
Kimia Kazemi ◽  
Negin Mozafari ◽  
Hajar Ashrafi ◽  
Pedram Rafiei ◽  
Amir Azadi
Keyword(s):  
Cell Proliferation ◽  
Mevalonate Pathway ◽  
Casein Kinase ◽  
Casein Kinase 2 ◽  
Interacting Protein ◽  
Akt Phosphorylation ◽  
Anticancer Properties ◽  
Proliferation And Apoptosis ◽  
Cellular Signaling Pathway ◽  
Hodgkin's Lymphomas

Background: Non-Hodgkin's lymphomas (NHL), derived from B- or T-cell, consist of a heterogeneous group of malignant lymphoproliferative disorders. Knockdown of Casein kinase 2 interacting protein-1 (CKIP-1) in NHL promoted cell proliferation and inhibited apoptosis via enhancing phosphorylated Protein Kinase B (PKB or AKT) expression. Statins are the class of drugs that inhibit the ratelimiting step of the mevalonate pathway, which is essential for the biosynthesis of various compounds, including cholesterol. Also, statins have anticancer properties being mediated by different mechanisms. Methods: A search on databases like Scopus and PubMed with keywords such as statin and non- Hodgkin's lymphomas was performed and Kyoto Encyclopedia of Genes and Genomes (KEGG) website was used to evaluate and reconfirm the involved cellular signaling pathway. Results: CKIP-1 is involved in the regulation of cell proliferation and apoptosis while plays an important role in many cancers. We can hypothesize that statins may increase the expression levels of CKIP-1 which could contribute to the reductions in phospho-AKT level. Hence, they may ameliorate the NHL patients via suppressing AKT phosphorylation and increasing CKIP- expression. Conclusion: Present review confirms the positive effect of statins on NHL by increasing CKIP-1 and reducing cell proliferation, subsequently.

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