scholarly journals Characterization of (−)-Matairesinol as a Potent Inhibitor of Casein Kinase I in Vitro

2003 ◽  
Vol 26 (3) ◽  
pp. 371-374 ◽  
Author(s):  
Takamasa Yokoyama ◽  
Maiko Okano ◽  
Toshiro Noshita ◽  
Shinji Funayama ◽  
Kenzo Ohtsuki
Keyword(s):  
Potent Inhibitor ◽  
Casein Kinase ◽  
Casein Kinase I

scholarly journals Casein kinase I-like protein kinases encoded by YCK1 and YCK2 are required for yeast morphogenesis.

1993 ◽  
Vol 13 (5) ◽  
pp. 2870-2881 ◽  
Author(s):  
L C Robinson ◽  
M M Menold ◽  
S Garrett ◽  
M R Culbertson
Keyword(s):  
Protein Kinase ◽  
Eukaryotic Cell ◽  
Casein Kinase ◽  
Temperature Sensitive ◽  
Protein Kinase Activity ◽  
Restrictive Temperature ◽  
Loss Of Function ◽  
Casein Kinase I ◽  
Yeast Saccharomyces Cerevisiae

Casein kinase I is an acidotropic protein kinase class that is widely distributed among eukaryotic cell types. In the yeast Saccharomyces cerevisiae, the casein kinase I isoform encoded by the gene pair YCK1 and YCK2 is a 60- to 62-kDa membrane-associated form. The Yck proteins perform functions essential for growth and division; either alone supports growth, but loss of function of both is lethal. We report here that casein kinase I-like activity is associated with a soluble Yck2-beta-galactosidase fusion protein in vitro and that thermolabile protein kinase activity is exhibited by a protein encoded by fusion of a temperature-sensitive yck2 allele with lacZ. Cells carrying the yck2-2ts allele arrest at restrictive temperature with multiple, elongated buds containing multiple nuclei. This phenotype suggests that the essential functions of the Yck proteins include roles in bud morphogenesis, possibly in control of cell growth polarity, and in cytokinesis or cell separation. Further, a genetic relationship between the yck2ts allele and deletion of CDC55 indicates that the function of Yck phosphorylation may be related to that of protein phosphatase 2A activity.

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 Characterization of Additional Casein Kinase I Sites in the C-Terminal “Tail” Region of Chicken and Rat Neurofilament-M

1997 ◽  
Vol 69 (4) ◽  
pp. 1729-1737 ◽  
Author(s):  
Gerry Shaw ◽  
Rehae Miller ◽  
Deng-Shun Wang ◽  
Dali Tang ◽  
Brian A. Hollander ◽  
...  
Keyword(s):  
Casein Kinase ◽  
Casein Kinase I ◽  
Tail Region

scholarly journals A New Sugarcane Cystatin Strongly Binds to Dental Enamel and Reduces Erosion

2017 ◽  
Vol 96 (9) ◽  
pp. 1051-1057 ◽  
Author(s):  
A.C. Santiago ◽  
Z.N. Khan ◽  
M.C. Miguel ◽  
C.C. Gironda ◽  
A. Soares-Costa ◽  
...  
Keyword(s):  
Potent Inhibitor ◽  
Surface Hardness ◽  
Dental Enamel ◽  
Reversible Inhibitors ◽  
Force Microscopy ◽  
Atomic Force ◽  
Enamel Erosion ◽  
Acquired Enamel Pellicle

Cystatin B was recently identified as an acid-resistant protein in acquired enamel pellicle; it could therefore be included in oral products to protect against caries and erosion. However, human recombinant cystatin is very expensive, and alternatives to its use are necessary. Phytocystatins are reversible inhibitors of cysteine peptidases that are found naturally in plants. In plants, they have several biological and physiological functions, such as the regulation of endogenous processes, defense against pathogens, and response to abiotic stress. Previous studies performed by our research group have reported high inhibitory activity and potential agricultural and medical applications of several sugarcane cystatins, including CaneCPI-1, CaneCPI-2, CaneCPI-3, and CaneCPI-4. In the present study, we report the characterization of a novel sugarcane cystatin, named CaneCPI-5. This cystatin was efficiently expressed in Escherichia coli, and inhibitory assays demonstrated that it was a potent inhibitor of human cathepsins B, K, and L ( Ki = 6.87, 0.49, and 0.34 nM, respectively). The ability of CaneCPI-5 to bind to dental enamel was evaluated using atomic force microscopy. Its capacity to protect against initial enamel erosion was also tested in vitro via changes in surface hardness. CaneCPI-5 showed a very large force of interaction with enamel (e.g., compared with mucin and casein) and significantly reduced initial enamel erosion. These results suggest that the inclusion of CaneCPIs in dental products might confer protection against enamel erosion.

scholarly journals Activation of C-Kinase η through Its Cholesterol-3-sulfate-Dependent Phosphorylation by Casein Kinase I in Vitro

2004 ◽  
Vol 27 (1) ◽  
pp. 109-112 ◽  
Author(s):  
Maiko Okano ◽  
Takamasa Yokoyama ◽  
Takahiro Miyanaga ◽  
Kenzo Ohtsuki
Keyword(s):  
Casein Kinase ◽  
Casein Kinase I

scholarly journals Respiratory Syncytial Virus M2-1 Protein Requires Phosphorylation for Efficient Function and Binds Viral RNA during Infection

2001 ◽  
Vol 75 (24) ◽  
pp. 12188-12197 ◽  
Author(s):  
Tara L. Cartee ◽  
Gail W. Wertz
Keyword(s):  
Protein Function ◽  
Consensus Sequence ◽  
Casein Kinase ◽  
Rnase A ◽  
Site Directed Mutagenesis ◽  
Binding Motif ◽  
Casein Kinase I ◽  
N Protein ◽  
Syncytial Virus

ABSTRACT The M2-1 protein of respiratory syncytial (RS) virus is a transcriptional processivity and antitermination factor. The M2-1 protein has a Cys3His1 zinc binding motif which is essential for function, is phosphorylated, and has been shown to interact with the RS virus nucleocapsid (N) protein. In the work reported here, we determined the sites at which the M2-1 protein was phosphorylated and investigated the importance of these phosphorylated residues for M2-1 function in transcription. By combining protease digestion, matrix-assisted laser desorption ionization–time of flight mass spectrometry, and site-directed mutagenesis, we identified the phosphorylated residues as serines 58 and 61, not threonine 56 and serine 58 as previously reported. Serines 58 and 61 and the surrounding amino acids are in a consensus sequence for phosphorylation by casein kinase I. Consistent with this, we showed that the unphosphorylated M2-1 protein synthesized in Escherichia coli could be phosphorylated in vitro by casein kinase I. The effect of eliminating phosphorylation by site-specific mutagenesis of serines 58 and 61 on the function of the M2-1 protein in transcription of RS virus subgenomic replicons was assayed. The activities of the M2-1 protein phosphorylation mutants in transcriptional antitermination were tested over a range of concentrations and were found to be substantially inhibited at all concentrations. The data show that phosphorylation is important for the M2-1 protein function in transcription. However, mutation of the M2-1 phosphorylation sites did not interfere with the ability of the M2-1 protein to interact with the N protein in transfected cells. The interaction of the M2-1 and N proteins in cotransfected cells was found to be sensitive to RNase A, indicating that the M2-1–N protein interaction was mediated via RNA. Furthermore, the M2-1 protein was shown to bind monocistronic and polycistronic RS virus mRNAs during infection.

scholarly journals The AP-3 Complex Required for Endosomal Synaptic Vesicle Biogenesis is Associated with a Casein Kinase Ια-Like Isoform

2000 ◽  
Vol 11 (8) ◽  
pp. 2591-2604 ◽  
Author(s):  
Victor V. Faundez ◽  
Regis B. Kelly
Keyword(s):  
Synaptic Vesicle ◽  
Synaptic Vesicles ◽  
Enzymatic Reaction ◽  
Casein Kinase ◽  
Small Gtpase ◽  
Casein Kinase I ◽  
Vesicle Membranes ◽  
Vesicle Biogenesis ◽  
Hinge Domain

The formation of small vesicles is mediated by cytoplasmic coats the assembly of which is regulated by the activity of GTPases, kinases, and phosphatases. A heterotetrameric AP-3 adaptor complex has been implicated in the formation of synaptic vesicles from PC12 endosomes ( Faundez et al., 1998 ). When the small GTPase ARF1 is prevented from hydrolyzing GTP, we can reconstitute AP-3 recruitment to synaptic vesicle membranes in an assembly reaction that requires temperatures above 15°C and the presence of ATP suggesting that an enzymatic step is involved in the coat assembly. We have now found an enzymatic reaction, the phosphorylation of the AP-3 adaptor complex, that is linked with synaptic vesicle coating. Phosphorylation occurs in the β3 subunit of the complex by a kinase similar to casein kinase 1α. The kinase copurifies with neuronal-specific AP-3. In vitro, purified casein kinase I selectively phosphorylates the β3A and β3B subunit at its hinge domain. Inhibiting the kinase hinders the recruitment of AP-3 to synaptic vesicles. The same inhibitors that prevent coat assembly in vitro also inhibit the formation of synaptic vesicles in PC12 cells. The data suggest, therefore, that the mechanism of AP-3-mediated vesiculation from neuroendocrine endosomes requires the phosphorylation of the adaptor complex at a step during or after AP-3 recruitment to membranes.

scholarly journals Casein Kinase Iγ2 Down-Regulates Trafficking of Ceramide in the Synthesis of Sphingomyelin

2009 ◽  
Vol 20 (1) ◽  
pp. 348-357 ◽  
Author(s):  
Nario Tomishige ◽  
Keigo Kumagai ◽  
Jun Kusuda ◽  
Masahiro Nishijima ◽  
Kentaro Hanada
Keyword(s):  
De Novo ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Casein Kinase ◽  
Repeat Motif ◽  
Casein Kinase I ◽  
Ovary Cells ◽  
Toxin Resistance ◽  
Transfer Protein

Intracellullar trafficking of lipids is fundamental to membrane biogenesis. For the synthesis of sphingomyelin, ceramide is transported from the endoplasmic reticulum to the Golgi apparatus by the ceramide transfer protein CERT. CERT is phosphorylated by protein kinase D at S132 and subsequently multiple times in a serine-repeat motif, resulting in its inactivation. However, the kinase involved in the multiple phosphorylation remains unclear. Here, we identify the γ2 isoform of casein kinase I (CKIγ2) as a kinase whose overexpression confers sphingomyelin-directed toxin-resistance to Chinese hamster ovary cells. In a transformant stably expressing CKIγ2, CERT was hyperphosphorylated, and the intracellular trafficking of ceramide was retarded, thereby reducing de novo sphingomyelin synthesis. The reduction in the synthesis of sphingomyelin caused by CKIγ2 was reversed by the expression of CERT mutants that are not hyperphosphorylated. Furthermore, CKIγ2 directly phosphorylated CERT in vitro. Among three γ isoforms, only knockdown of γ2 isoform caused drastic changes in the ratio of hypo- to hyperphosphorylated form of CERT in HeLa cells. These results indicate that CKIγ2 hyperphosphorylates the serine-repeat motif of CERT, thereby inactivating CERT and down-regulating the synthesis of sphingomyelin.

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