Polyamine binding activity of casein kinase II

Filhol, Odile; Cochet, Claude; Delagoutte, Thierry; Chambaz, E.M.

doi:10.1016/s0006-291x(05)81157-x

Cited by 48 publications

(23 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The polybasic peptides appear to react with an acidic cluster in residues 55-64 of the 1-subunit (Boldyreff et al, 1993;Meggio et al, 1994). The isolated atsubunit is not activated by polyamines (Filhol et al, 1991).…”

Section: (C) Other Bone Ncpsmentioning

confidence: 98%

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Veis

Sfeir

1997

Critical Reviews in Oral Biology & Medicine

View full text Add to dashboard Cite

The extracellular matrix of the connective tissue contains non-collagenous proteins (NCP) which are acidic in character. The NCP of mineralizing systems (bone, dentin) differ from those of the non-mineralizing systems (skin, tendon) in that the mineralized tissue NCP are frequently phosphorylated. The phosphorylated proteins have been implicated in various aspects of the mineralization process. Thus, it is of interest to consider the mechanism and regulation of phosphorylation of the major matrix NCP. The majority of the phosphorylation takes place at Ser or Thr residues embedded within acidic sequences, and therefore are targets for casein kinase I (CKI ) or casein kinase 11 (CK2)-like kinases. CKI and CK2 are distantly related members of the protein kinase family. They are ubiquitous, constitutively active, second-messenger-independent kinases. CKI is found in a variety of isoforms, all homologous to the cx-subunit of the protein kinase family. It acts as a monomer. The active form of CK2 is a tetrameric holoenzyme, with 2 cx catalytic subunits and 2 ( regulatory subunits. The CK2 ac has activity alone, but the holoenzyme is four-to five-fold that activity. CK2 can use either ATP or GTP as the phosphate donor, but CK 1 can use only ATP. The CK2 activity which phosphorylates the mineralized tissue NCP appears to be localized to membraneassociated cell fractions, and is present in the endoplasmic reticulum and Golgi compartments in osteoblasts, where phosphorylation of the secreted proteins appears to take place as co-and post-translational processes. Data Bone and dentin are tissues in which mineral deposits of carbonate apatite form in an orderly fashion within a pre-formed collagen fibril matrix. Structural studies clearly show that the majority of the mineral phase is composed of carbonate-apatite crystals, whose crystal c-axes are aligned with the fibril axes of the collagen fibrils (FittonJackson, 1957;Glimcher and Krane, 1968;Glimcher, 1976;Weiner and Traub, 1986;Arsenault, 1988;Arsenault et al, 1991;Landis et al., 1992). Although much of the early work attempted to show that the collagen fibrils were responsible for the placement and induction of mineral deposition, this proposition was never verified. Instead, attention began to focus on the non-collagenous protein components of the matrix (Herring and Kent, 1963;Schlueter and Veis, 1964;Veis and Schlueter, 1964;Spector and Glimcher, 1972;Veis et al., 1972;Glimcher, 1976), especially since it was recognized that, as a class, the non-collagenous extracellular proteins (NCP) shared a common char360Crit Rev Oral Biol Med 8(4)

show abstract

Section: (C) Other Bone Ncpsmentioning

confidence: 98%

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Veis

Sfeir

1997

Critical Reviews in Oral Biology & Medicine

View full text Add to dashboard Cite

show abstract

“…Assays were performed at room temperature for 5 minutes before termination by the addition of 60 mL of 4% trichloroacetic acid. Incorporation of 32 P in the peptide substrate was determined as previously described (23).…”

Section: Ck2 Phosphorylation Assaysmentioning

confidence: 99%

Antitumor Activity of Pyridocarbazole and Benzopyridoindole Derivatives that Inhibit Protein Kinase CK2

et al. 2010

Self Cite

View full text Add to dashboard Cite

The alkyloid compound ellipticine derived from the berrywood tree is a topoisomerase II poison that is used in ovarian and breast cancer treatment. In this study, we report the identification of ellipticine derivatives and their tetracyclic angular benzopyridoindole analogues as novel ATP-competitive inhibitors of the protein kinase CK2. In vitro and in vivo assays showed that these compounds have a good pharmacologic profile, causing a marked inhibition of CK2 activity associated with cell cycle arrest and apoptosis in human cancer cells. Further, in vivo assays demonstrate antitumor activity in a mouse xenograft model of human glioblastoma. Finally, crystal structures of CK2-inhibitor complex provide structural insights on the molecular basis of CK2 inhibition. Our work lays the foundation for development of clinically useful CK2 inhibitors derived from a well-studied scaffold with suitable pharmacokinetics parameters. Cancer Res; 70(23); 9865-74. Ó2010 AACR.

show abstract

“…In vitro studies with recombinant subunits suggest that the 1 subunit stabilizes the a subunit, mediates interaction with the basic compounds such as polyamines that stimulate casein kinase activity, and may lower the Km for substrates (31,32,40,108). However, it is clear that the 13 (27,43,44) (Table 1 and data not shown).…”

Section: Er-------------------90mentioning

confidence: 99%

Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle.

Kikkawa¹,

Mann²,

Firtel³

et al. 1992

Mol. Cell. Biol.

View full text Add to dashboard Cite

A Dictyostelium discoideum cDNA encoding an a-type subunit of casein kinase If was isolated, and its cDNA was used to study developmental expression of casein kinase Hi during the Dictyostelium life cycle. The 1.3-kb cDNA insert contained an open reading frame of 337 amino acids (Mr 39,900 Casein kinase II is a ubiquitous protein-serine/threonine kinase in eukaryotic cells that catalyzes the phosphorylation of many protein substrates and has been regarded as a second-messenger-independent protein kinase (reviewed in references 27, 43, 82, and 109). When isolated from most species, this enzyme is composed of an a subunit (37 to 44 kDa) and a v subunit (24 to 28 kDa) and exists as an a212tetramer. The primary amino acid sequences of the a and 13 subunits of several species, which have been determined by molecular cloning and by direct protein sequence analysis, are well conserved among the species thus far studied (8,14,25,45,47,49,51,58,66,69,80,83,87,96,104,106). The a subunit contains a protein kinase domain that is homologous to the catalytic domain of other protein kinases (42), whereas the 13 subunit shows no significant homology Vv ith other proteins except the Drosophila melanogaster steijate gene products (67). The 1 subunit is presumed to regulate the catalytic activity (17), although the precise role of this subunit is not clear (59). There is some evidence that the 13 subunit stabilizes the a subunit, but it is not required for the catalytic activity of the a subunit (32,40,108 (80). In yeast cells, disruption of both a-subunit genes causes inviability, whereas disruption of either one of these genes alone has no detectable phenotype. This finding indicates that at least one of the a-type subunits is essential and that the two a-type subunits can complement one another in S. cerevisiae (87).Casein kinase II is detected in both the nucleus and the cytoplasm by fractionation experiments (43, 109). Immunolocalization studies have yielded somewhat conflicting results about the subcellular localization of casein kinase II (30,60,112). In one study, all three subunits were found to be predominantly nuclear under all conditions (60), whereas in the another study, the a and 13 subunits were found to be mainly cytoplasmic in interphase and the a' subunit was nuclear in G1 and cytoplasmic in S phase (112). In the third study, casein kinase II was found in the nucleus of growing cells but distributed in the nucleus and cytoplasm in quiescent cells (30). A role for casein kinase II in the nucleus is suggested by recent studies showing that a number of the nuclear proteins, such as c-Myc (72), Max (7), c-Myb (71), serum response factor (74, 79), c-Fos (12), c-Jun (64), DNA ligase (90), topoisomerase II (10), the p53 tumor suppressor protein (81), the adenovirus ElA protein (12), the human papillomavirus E7 protein (6,35), and the simian virus 40 large T antigen (41, 59), are phosphorylated by casein kinase II in vitro at physiological sites and that the DNA-binding activity of some of these nuclear proteins is regu...

show abstract

Polyamine binding activity of casein kinase II

Cited by 48 publications

References 13 publications

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Phosphorylation of the Proteins of the Extracellular Matrix of Mineralized Tissues By Casein Kinase-Like Activity

Antitumor Activity of Pyridocarbazole and Benzopyridoindole Derivatives that Inhibit Protein Kinase CK2

Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle.

Contact Info

Product

Resources

About