Casein kinases regulation

There is growing evidence that clock proteins are regulated dynamically in both temporal (production and degradation) and spatial (nuclear and cytoplasmic) dimensions. The phosphorylation of mPERl and mPER2 by casein kinase le (CKIe) is known as an important step for the accumulation of negatively active clock proteins (Lowrey et al 2000) as in Drosophila (Kloss et al 1998). 

Yang Y, Cheng P, Liu Y 2002 Regulation of Neurospora circadian clock by casein kinase II. Genes Dev 16 994-1006... 

Ishida N, Miyazaki K, Sakai T 2001 Circadian rhythm biochemistry from protein degradation to sleep and mating. Biochem Biophys Res Commun 286 1—5 Kloss B, Price JL, Saez L et al 1998 The Drosophila clock gene double-time encodes a protein closely related to human casein kinase lepsilon. Cell 94 97—107 Lau LF, Nathans D 1987 Expression of a set of growth-related immediate early genes in BALE/ c 3T3 cells coordinate regulation with c-fos or c-myc. Proc Natl Acad Sci USA 84 1182-1186... 

Vielhaber E, Eide E, Rivers A, Gao ZH, Virshup DM 2000 Nuclear entry of the circadian regulator mPERl is controlled by mammalian casein kinase I epsilon. Mol Cell Biol 20 4888-4899... 

The flavonoid crysin and benzothiophenes have been shown to inhibit casein kinase II (CKII), a cellular protein that may regulate HIV-1 transcription by phosphorylating (other) cellular proteins involved in the HIV-1 transcription transactivation process. This mechanism of action is independent of the nuclear factor kB-driven transcription pathway. Thus, flavonoids interfere with HIV-1 transcription and hence prevent HIV expression in latently infected cells. Their specificity and usefulness as HIV transcription inhibitors remain to be assessed. 

Kafadar KA, Zhu H, Snyder M, Cyert MS. Negative regulation of calcineurin signaling by Hrr25p, a yeast homolog of casein kinase I. Genes Dev 2003 17 2698-2708. 

Desdouits F, Siciliano JC, Greengard P, Girault JA (1995a) Dopamine- and cAMP-regulated phosphoprotein DARPP-32 phosphorylation of Ser-137 by casein kinase I inhibits dephosphorylation of Thr-34 by... 

Desdouits F, Cohen D, Nairn AC, Greengard P, Girault JA (1995b) Phosphorylation of DARPP-32, a dopamine-and cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo. J Biol Chem 270 8772-8778. 

Liu F, Ma XH, Ule J, Bibb JA, Nishi A, DeMaggio AJ, Yan Z, Nairn AC, Greengard P (2001a) Regulation of cyclin-dependent kinase 5 and casein kinase 1 by metabotropic glutamate receptors. Proc Natl Acad Sci USA 98 11062-11068. 

Cyclic nucleotide regulated protein kinase family = Adenylyl cyclases = A-kinase anchor proteins = Atypical PKCs = Atrial natriuretic peptide = Adenosine 5 -triphosphate = Brain natriuretic peptide = Ca Vcalmodulin-dependent kinases = Cyclin-dependent kinases = Ca -dependent protein kinase = Casein kinase I = Casein kinase II = Dcd-like kinase... 

CD. Cooper, P.D. Lampe, Casein kinase 1 regulates connexin-43 gap junction assembly, J Biol Chem 277,4962-44968(2003). 

K. Cieslik, C.-M. Lee, J. Tang, K.K. Wu, Transcriptional regulation of endothelial nitric-oxide synthase by an interaction between casein kinase 2 and protein phosphatase 2A, J Biol Chem 274, 34669-34675 (1999). 

FK506-binding protein FKBP52 by casein kinase II regulation of HSP90-bind-ing activity of FKBP52. Proc Natl Acad Sci USA 94(26) 14500-14505, 1997. 

The lithium cation (Li" ) has been shown to inhibit GSK-3P with a potency around 2 mM IC50 (3.3 mM K ) and, although weak, this concentration is achievable clinically, thus offering the potential as a useful therapeutic. Other than GSK-3, Ii+ has been shown to also inhibit polyphosphate 1-phosphatase, inositol monophosphatase, casein kinase-II (CKII), MAP kinase-activated protein kinase-2 (MAPKAP-K2) and p38-regulated/activated kinase (PRAK) as well as activating, in cells, PI3-kinase/PKB and c-jun N-terminal kinase (JNK) [63-66]. Naturally this polypharmacology complicates the interpretation between target and function of Li+. 

Regulation of glycogen synthase by multisite phosphorylation. The location of phosphorylation sites ( ) and the protein kinases that phosphorylate at these sites (boxes) are shown. Phosphorylations occur only at N- and C-terminal regions of the enzymes, as indicated by CB-N and CB-C, respectively. The single-letter abbreviations for amino acids are used (see Chapter 2). cAMP-PK = cyclic AMP-dependent protein kinase CAM-MPK = Ca +/calmodulin-dependent multiprotein kinase PhK = phosphorylase kinase GSK = glycogen synthase kinase CK = casein kinase NIO-PK = A novel protein kinase. [Reproduced with permission from P. Cohen, Protein phosphorylation and hormone action. Proc. R. Soc. Lonrf. (Biol.) 234, 115(1988).]... 

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