Biochemical Characterization of Casein Kinase II as a Protein Kinase Responsible for Stimulation of HIV-1 Protease in Vitro

2000 ◽  
Vol 275 (2) ◽  
pp. 434-439 ◽  
Author(s):  
Eiji Haneda ◽  
Teisuke Furuya ◽  
Shigeru Asai ◽  
Yuko Morikawa ◽  
Kenzo Ohtsuki
Keyword(s):  
Protein Kinase ◽  
Biochemical Characterization ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Hiv 1 ◽  
Stimulation Of

Biochemical characterization of HIV-1 Rev as a potent activator of casein kinase II in vitro

FEBS Letters ◽  
1998 ◽  
Vol 428 (3) ◽  
pp. 235-240 ◽  
Author(s):  
Kenzo Ohtsuki ◽  
Toshiro Maekawa ◽  
Shigeyoshi Harada ◽  
Atsushi Karino ◽  
Yuko Morikawa ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Hiv 1

scholarly journals Casein kinase II(CK-II)-Mediated Stimulation of HIV-1 Reverse Transcriptase Activity and Characterization of Selective Inhibitors in Vitro.

1999 ◽  
Vol 22 (10) ◽  
pp. 1122-1126 ◽  
Author(s):  
Shigeyoshi HARADA ◽  
Eiji HANEDA ◽  
Toshiro MAEKAWA ◽  
Yuko MORIKAWA ◽  
Shinji FUNAYAMA ◽  
...  
Keyword(s):  
Reverse Transcriptase ◽  
Casein Kinase Ii ◽  
Reverse Transcriptase Activity ◽  
Casein Kinase ◽  
Selective Inhibitors ◽  
Transcriptase Activity ◽  
Hiv 1 ◽  
Stimulation Of

Identification of Glycyrrhizin-Binding Protein Kinase as Casein Kinase II and Characterization of Its Associated Phosphate Acceptors in Mouse Liver

1996 ◽  
Vol 227 (1) ◽  
pp. 102-109 ◽  
Author(s):  
Shigeyoshi Harada ◽  
Atsushi Karino ◽  
Yoshihito Shimoyama ◽  
Fazel Shamsa ◽  
Kenzo Ohtsuki
Keyword(s):  
Protein Kinase ◽  
Mouse Liver ◽  
Binding Protein ◽  
Casein Kinase Ii ◽  
Casein Kinase

scholarly journals DNA repair protein O6-alkylguanine-DNA alkyltransferase is phosphorylated by two distinct and novel protein kinases in human brain tumour cells

2000 ◽  
Vol 351 (2) ◽  
pp. 393-402 ◽  
Author(s):  
Srinivas R. S. MULLAPUDI ◽  
Francis ALI-OSMAN ◽  
Jiang SHOU ◽  
Kalkunte S. SRIVENUGOPAL
Keyword(s):  
Dna Repair ◽  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Protein Kinases ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Biochemical Modulation ◽  
Cell Extracts ◽  
Dna Alkyltransferase

We showed recently that human O6-alkylguanine-DNA alkyltransferase (AGT), an important target for improving cancer chemotherapy, is a phosphoprotein and that phosphorylation inhibits its activity [Srivenugopal, Mullapudi, Shou, Hazra and Ali-Osman (2000) Cancer Res. 60, 282–287]. In the present study we characterized the cellular kinases that phosphorylate AGT in the human medulloblastoma cell line HBT228. Crude cell extracts used Mg2+ more efficiently than Mn2+ for phosphorylating human recombinant AGT (rAGT) protein. Both [γ-32P]ATP and [γ-32P]GTP served as phosphate donors, with the former being twice as efficient. Specific components known to activate protein kinase A, protein kinase C and calmodulin-dependent kinases did not stimulate the phosphorylation of rAGT. Phosphoaminoacid analysis after reaction in vitro with ATP or GTP showed that AGT was modified at the same amino acids (serine, threonine and tyrosine) as in intact HBT228 cells. Although some of these properties pointed to casein kinase II as a candidate enzyme, known inhibitors and activators of casein kinase II did not affect rAGT phosphorylation. Fractionation of the cell extracts on poly(Glu/Tyr)-Sepharose resulted in the adsorption of an AGT kinase that modified the tyrosine residues and the exclusion of a fraction that phosphorylated AGT on serine and threonine residues. In-gel kinase assays after SDS/PAGE and non-denaturing PAGE revealed the presence of two AGT kinases of 75 and 130kDa in HBT228 cells. The partly purified tyrosine kinase, identified as the 130kDa enzyme by the same assays, was strongly inhibited by tyrphostin 25 but not by genestein. The tyrosine kinase used ATP or GTP to phosphorylate the AGT protein; this reaction inhibited the DNA repair activity of AGT. Evidence that the kinases might physically associate with AGT in cells was also provided. These results demonstrate that two novel cellular protein kinases, a tyrosine kinase and a serine/threonine kinase, both capable of using GTP as a donor, phosphorylate the AGT protein and affect its function. The new kinases might serve as potential targets for strengthening the biochemical modulation of AGT in human tumours.

scholarly journals A casein kinase II-related activity is involved in phosphorylation of microtubule-associated protein MAP-1B during neuroblastoma cell differentiation.

1988 ◽  
Vol 106 (6) ◽  
pp. 2057-2065 ◽  
Author(s):  
J Díaz-Nido ◽  
L Serrano ◽  
E Méndez ◽  
J Avila
Keyword(s):  
Protein Kinase ◽  
Neuroblastoma Cells ◽  
Casein Kinase Ii ◽  
Casein Kinase ◽  
Related Activity ◽  
Dependent Protein Kinase ◽  
Protein Map ◽  
Dependent Protein

A neuroblastoma protein related to the brain microtubule-associated protein, MAP-1B, as determined by immunoprecipitation and coassembly with brain microtubules, becomes phosphorylated when N2A mouse neuroblastoma cells are induced to generate microtubule-containing neurites. To characterize the protein kinases that may be involved in this in vivo phosphorylation of MAP-1B, we have studied its in vitro phosphorylation. In brain microtubule protein, MAP-1B appears to be phosphorylated in vitro by an endogenous casein kinase II-like activity which also phosphorylates the related protein MAP-1A but scarcely phosphorylates MAP-2. A similar kinase activity has been detected in cell-free extracts of differentiating N2A cells. Using brain MAP preparations devoid of endogenous kinase activities and different purified protein kinases, we have found that MAP-1B is barely phosphorylated by cAMP-dependent protein kinase, Ca/calmodulin-dependent protein kinase, or Ca/phospholipid-dependent protein kinase whereas MAP-1B is one of the preferred substrates, together with MAP-1A, for casein kinase II. Brain MAP-1B phosphorylated in vitro by casein kinase II efficiently coassembles with microtubule proteins in the same way as in vivo phosphorylated MAP-1B from neuroblastoma cells. Furthermore, the phosphopeptide patterns of brain MAP-1B phosphorylated in vitro by either purified casein kinase II or an extract obtained from differentiating neuroblastoma cells are identical to each other and similar to that of in vivo phosphorylated neuroblastoma MAP-1B. Thus, we suggest that the observed phosphorylation of a protein identified as MAP-1B during neurite outgrowth is mainly due to the activation of a casein kinase II-related activity in differentiating neuroblastoma cells. This kinase activity, previously implicated in beta-tubulin phosphorylation (Serrano, L., J. Díaz-Nido, F. Wandosell, and J. Avila, 1987. J. Cell Biol. 105: 1731-1739), may consequently have an important role in posttranslational modifications of microtubule proteins required for neuronal differentiation.

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