Casein Kinase I in the Mammalian Circadian Clock

Eide, Erik J.; Kang, Heeseog; Crapo, Stephanie; Gallego, Mónica; Virshup, David M.

doi:10.1016/s0076-6879(05)93019-x

Cited by 59 publications

(37 citation statements)

References 14 publications

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“…In addition, casein kinase I epsilon (CKIε) phosphorylates the PER proteins and, thereby, enhances their instability and degradation [44][45][46]. CKIε also phosphorylates and partially activates BMAL1 [47].…”

Section: The Molecular Clockmentioning

confidence: 99%

Circadian Signatures in Rat Liver: From Gene Expression to Pathways

Olds¹

2014

Sleep, Circadian Rhythms, and Metabolism

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Obesity has become a serious public health problem and a major risk factor for the development of illnesses, such as insulin resistance and hypertension. Attempts to understand the causes of obesity and develop new therapeutic strategies have mostly focused on caloric intake and energy expenditure. Recent studies have shown that the circadian clock controls energy homeostasis by regulating the circadian expression and/or activity of enzymes, hormones, and transport systems involved in metabolism. Moreover, disruption of circadian rhythms leads to obesity and metabolic disorders. Therefore, it is plausible that resetting of the circadian clock can be used as a new approach to attenuate obesity. Feeding regimens, such as restricted feeding (RF), calorie restriction (CR), and intermittent fasting (IF), provide a time cue and reset the circadian clock and lead to better health. In contrast, high-fat (HF) diet leads to disrupted circadian expression of metabolic factors and obesity. This paper focuses on circadian rhythms and their link to obesity.

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Section: The Molecular Clockmentioning

confidence: 99%

Circadian Signatures in Rat Liver: From Gene Expression to Pathways

Olds¹

2014

Sleep, Circadian Rhythms, and Metabolism

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“…14 The protein kinases CK1ε and CKIδ phosphorylate elements belonging to both positive and negative limbs by modulating the nucleocytoplasmic shuttling of core clock elements and thereby their transcriptional activity. 31,32 Chromatin modifications through acetylation, deacetylation and methylation of histones present in promoter region of core clock genes, participate in the regulation of oscillating transcription. Clock gene possesses intrinsic histone acetyltransferase activity and the activation of core clock genes by BMAL1/CLOCK heterodimers is indeed preferentially coupled to histone acetylation.…”

Section: Circadian Molecular Oscillatorsmentioning

confidence: 99%

Cell “circadian” cycle: New role for mammalian core clock genes

Borgs¹,

Beukelaers²,

Vandenbosch³

et al. 2009

Cell Cycle

109

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In mammals, 24 hours rhythms are organized as a biochemical network of molecular clocks that are operative in all tissues, with the master clock residing in the hypothalamic suprachiasmatic nucleus (SCN). The core pacemakers of these clocks consist of auto-regulatory transcriptional/post-transcriptional feedback loops. Several lines of evidence suggest the existence of a crosstalk between molecules that are responsible for the generation of circadian rhythms and molecules that control the cell cycle progression. In addition, highly specialized cell cycle checkpoints involved in DNA repair after damage seem also, at least in part, mediated by clock proteins. Recent studies have also highlighted a putative connection between clock protein dysfunction and cancer progression. This review discusses the intimate relation that exists between cell cycle progression and components of the circadian machinery.

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“…Recombinant wild-type and mutant CERTs expressed in E. coli cells were purified with a Talon Co 2ϩ affinity column (Clontech) as described previously (Hanada et al, 2003), and the in vitro kinase assay was performed by a modification of previously described methods (Gietzen et al, 1999;Eide et al, 2005). The reactions were performed in 30 l of kinase buffer containing 200 M ATP, 1 mM dithiothreitol, 50 g/ml BSA, 2 Ci of [␥-…”

Section: In Vitro Kinase Assaymentioning

confidence: 99%

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

Tomishige

Kumagai

Kusuda

et al. 2009

MBoC

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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 ␥2 isoform of casein kinase I (CKI␥2) as a kinase whose overexpression confers sphingomyelin-directed toxin-resistance to Chinese hamster ovary cells. In a transformant stably expressing CKI␥2, 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 CKI␥2 was reversed by the expression of CERT mutants that are not hyperphosphorylated. Furthermore, CKI␥2 directly phosphorylated CERT in vitro. Among three ␥ isoforms, only knockdown of ␥2 isoform caused drastic changes in the ratio of hypo-to hyperphosphorylated form of CERT in HeLa cells. These results indicate that CKI␥2 hyperphosphorylates the serine-repeat motif of CERT, thereby inactivating CERT and down-regulating the synthesis of sphingomyelin.

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Casein Kinase I in the Mammalian Circadian Clock

Cited by 59 publications

References 14 publications

Circadian Signatures in Rat Liver: From Gene Expression to Pathways

Circadian Signatures in Rat Liver: From Gene Expression to Pathways

Cell “circadian” cycle: New role for mammalian core clock genes

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

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