The casein kinase 1 family: participation in multiple cellular processes in eukaryotes

Knippschild, Uwe; Gocht, Andreas; Wolff, Sonja; Huber, Nadine; Löhler, Jürgen; Stöter, Martin

doi:10.1016/j.cellsig.2004.12.011

Cited by 495 publications

(566 citation statements)

References 229 publications

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“…Deregulated expression of CK1 has been observed in multiple cancer types. For example, elevated expression or activity of CK1 was detected in acute myeloblastic leukemia, and somatic mutations associated with increased expression of CK1e were detected in ductal carcinoma (reviewed by Knippschild et al, 2005). Our results strongly implicate PML in the proper regulation of Thr18 phosphorylation.…”

Section: Pml Regulates the Phosphorylation Of P53 By Ck1mentioning

confidence: 51%

“…Casein kinase 1 is a family of serine/threonine protein kinase, consisting of multiple isoforms encoded by separate genes (CK1a, b, g1, g2, g3, d and e) and has been implicated in the regulation of various cellular functions, including membrane transport, cell division, apoptosis, chromosome segregation and the circadian rhythm (reviewed by Knippschild et al, 2005). A CK1-related kinase in yeast, hrr25, is essential for DNA repair and can be complemented by its mammalian homologs CK1d and e isoforms (Hoekstra et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

“…p53 is a substrate for both isoforms, linking them to DNA repair and cell-cycle regulation also in mammalian cells (Knippschild et al, 1997). CK1d/e phosphorylates mouse p53 on Ser4, 6 and 9 and human p53 on Ser9 and Thr18 (reviewed by Knippschild et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

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PML enhances the regulation of p53 by CK1 in response to DNA damage

et al. 2008

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In response to stress, p53 is accumulated and activated to induce appropriate growth inhibitory responses. This requires the release of p53 from the constraints of its negative regulators Mdm2 and Mdm4. A key event in this dissociation is the phosphorylation of p53 at threonine residue (Thr18) within the Mdm2/4-binding domain. Casein kinase 1 (CK1) plays a major role in this phosphorylation. The promyelocytic leukemia protein (PML) regulates certain modifications of p53 in response to DNA damage. Here, we investigated the role of PML in the regulation of Thr18 phosphorylation. We found that PML enhances Thr18 phosphorylation of endogenous p53 in response to stress. On DNA damage, CK1 accumulates in the cell, with a proportion concentrated in the nucleus together with p53 and PML. Furthermore, CK1 interacts with endogenous p53 and PML, and this interaction is enhanced by genotoxic stress. Inhibition of CK1 impairs the protection of p53 by PML from Mdm2-mediated degradation. Our findings support a role for PML in the regulation of p53 by CK1. We propose that following DNA damage, PML facilitates Thr18 phosphorylation by recruiting p53 and CK1 into PML nuclear bodies, thereby protecting p53 from inhibition by Mdm2, leading to p53 activation.

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Section: Pml Regulates the Phosphorylation Of P53 By Ck1mentioning

confidence: 51%

Section: Introductionmentioning

confidence: 99%

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PML enhances the regulation of p53 by CK1 in response to DNA damage

et al. 2008

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“…This complex binds to Ebox sequences in the promoters of many genes including the Period (Per) and Cryptochrome (Cry) genes. The PER and CRY proteins are translated in the cytoplasm, and are phosphorylated by Casein Kinase I ε and δ (CK1) and Glycogen Synthase Kinase 3β (GSK3β), leading to changes in their stability, association, and nuclear entry (Harms et al, 2003;Iitaka et al, 2005;Knippschild et al, 2005;Kurabayashi et al, 2006). Upon entering the nucleus, they can repress the actions of CLOCK/BMAL1, thus creating a negative feedback loop.…”

Section: The Molecular Clockmentioning

confidence: 99%

Circadian genes, rhythms and the biology of mood disorders

McClung

2007

Pharmacology & Therapeutics

572

386

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For many years, researchers have suggested that abnormalities in circadian rhythms may underlie the development of mood disorders such as bipolar disorder, major depression and seasonal affective disorder. Furthermore, some of the treatments that are currently employed to treat mood disorders are thought to act by shifting or "resetting" the circadian clock, including total sleep deprivation and bright light therapy. There is also reason to suspect that many of the mood stabilizers and antidepressants used to treat these disorders may derive at least some of their therapeutic efficacy by affecting the circadian clock. Recent genetic, molecular and behavioral studies implicate individual genes that make up the clock in mood regulation. As well, important functions of these genes in brain regions and neurotransmitter systems associated with mood regulation is becoming apparent. In this review, the evidence linking circadian rhythms and mood disorders, and what is known about the underlying biology of this association, is presented.

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“…It is known that the mammalian CKI isoforms (a, b1, b2, g1, g2, d, e) can phosphorylate many different substrates, among which there are key regulatory proteins involved in control of cell proliferation and differentiation, crucial events during cancer progression (Knippschild et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility

Garzia¹,

D’Angelo²,

Amoresano

et al. 2007

Oncogene

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The combination of an increase in the cAMP-phosphodiesterase activity of h-prune and its interaction with nm23-H1 have been shown to be key steps in the induction of cellular motility in breast cancer cells. Here we present the molecular mechanisms of this interaction. The region of the nm23-h-prune interaction lies between S120 and S125 of nm23, where missense mutants show impaired binding; this region has been highly conserved throughout evolution, and can undergo serine phosphorylation by casein kinase I. Thus, the casein kinase I d-e specific inhibitor IC261 impairs the formation of the nm23-hprune complex, which translates 'in vitro' into inhibition of cellular motility in a breast cancer cellular model. A competitive permeable peptide containing the region for phosphorylation by casein kinase I impairs cellular motility to the same extent as IC261. The identification of these two modes of inhibition of formation of the nm23-H1-h-prune protein complex pave the way toward new challenges, including translational studies using IC261 or this competitive peptide 'in vivo' to inhibit cellular motility induced by nm23-H1-h-prune complex formation during progression of breast cancer.

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The casein kinase 1 family: participation in multiple cellular processes in eukaryotes

Cited by 495 publications

References 229 publications

PML enhances the regulation of p53 by CK1 in response to DNA damage

PML enhances the regulation of p53 by CK1 in response to DNA damage

Circadian genes, rhythms and the biology of mood disorders

Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility

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