Biological functions of casein kinase 1 isoforms and putative roles in tumorigenesis

Schittek, Birgit; Sinnberg, Tobias

doi:10.1186/1476-4598-13-231

Cited by 196 publications

(240 citation statements)

References 106 publications

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“…The CK1α localization on microtubules decreases as cells progress to telophase. In telophase, CK1α is localized to the centrosome, but there is no localization to midbody microtubules [29]. Taken together, these results suggest that CK1α relocalizes from vesicular structures to the centrosome and aster microtubules in prophase and with kinetochore microtubules and possibly other interpolar microtubules during mitosis [30].…”

Section: Expression and Subcellular Localization Of Ck1supporting

confidence: 60%

The Role of Casein Kinase 1 in Meiosis

Zhao¹,

Liang²

2016

J Down Syndr Chr Abnorm

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Section: Expression and Subcellular Localization Of Ck1supporting

confidence: 60%

The Role of Casein Kinase 1 in Meiosis

Zhao¹,

Liang²

2016

J Down Syndr Chr Abnorm

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“…Up to now, more than 140 in vitro and in vivo substrates of CK1 have been reported, including proteins involved in cell cycle, apoptosis, DNA repair, mitochondrial function and signal transduction. The important role of CK1 family members has been documented by reports linking CK1 isoforms to modulation of key regulatory proteins such as p53, MDM2 and β-catenin, all of which act as signal integration molecules in stress situations and are connected to tumorigenesis (Schittek and Sinnberg, 2014).…”

Section: Introductionmentioning

confidence: 99%

HIF-2α phosphorylation by CK1δ promotes erythropoietin secretion in liver cancer cells under hypoxia

Pangou

Befani

Mylonis

et al. 2016

Journal of Cell Science

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Hypoxia inducible factor 2 (HIF-2) is a transcriptional activator implicated in the cellular response to hypoxia. Regulation of its inducible subunit, HIF-2α (also known as EPAS1), involves posttranslational modifications. Here, we demonstrate that casein kinase 1δ (CK1δ; also known as CSNK1D) phosphorylates HIF-2α at Ser383 and Thr528 in vitro. We found that disruption of these phosphorylation sites, and silencing or chemical inhibition of CK1δ, reduced the expression of HIF-2 target genes and the secretion of erythropoietin (EPO) in two hepatic cancer cell lines, Huh7 and HepG2, without affecting the levels of HIF-2α protein expression. Furthermore, when CK1δ-dependent phosphorylation of HIF-2α was inhibited, we observed substantial cytoplasmic mislocalization of HIF-2α, which was reversed upon the addition of the nuclear protein export inhibitor leptomycin B. Taken together, these data suggest that CK1δ enhances EPO secretion from liver cancer cells under hypoxia by modifying HIF-2α and promoting its nuclear accumulation. This modification represents a new mechanism of HIF-2 regulation that might allow HIF isoforms to undertake differing functions.

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“…In vertebrates, seven CK1 isoforms (α, β, γ1, γ2, γ3, δ and ε) and several splice variants for CK1α, δ, ε and γ3 have been identified [136] . This family of kinases has been shown to phosphorylate key regulatory molecules involved in a wide array of cellular activities such as cell cycle, cytokinesis, chromosome and microtubule dynamics and transcription and translation [136] . NFAT5 nucleocytoplasmic trafficking is regulated by the dual phosphorylation of serine 155 and 158 [27] .…”

Section: Glycogen Synthase Kinase 3β Casein Kinase 1 and 5' -Ampkmentioning

confidence: 99%

“…It would be interesting to know the effect of high NaCl on NFAT5 activity in these cells. CK is a group of serine/threonine kinases that can be divided into CK1 and CK2 families based on their high homology in their catalytic domains [136] . In vertebrates, seven CK1 isoforms (α, β, γ1, γ2, γ3, δ and ε) and several splice variants for CK1α, δ, ε and γ3 have been identified [136] .…”

Section: Glycogen Synthase Kinase 3β Casein Kinase 1 and 5' -Ampkmentioning

confidence: 99%

“…CK is a group of serine/threonine kinases that can be divided into CK1 and CK2 families based on their high homology in their catalytic domains [136] . In vertebrates, seven CK1 isoforms (α, β, γ1, γ2, γ3, δ and ε) and several splice variants for CK1α, δ, ε and γ3 have been identified [136] . This family of kinases has been shown to phosphorylate key regulatory molecules involved in a wide array of cellular activities such as cell cycle, cytokinesis, chromosome and microtubule dynamics and transcription and translation [136] .…”

Section: Glycogen Synthase Kinase 3β Casein Kinase 1 and 5' -Ampkmentioning

confidence: 99%

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How do kinases contribute to tonicity-dependent regulation of the transcription factor NFAT5?

Zhou

2016

WJN

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NFAT5 plays a critical role in maintaining the renal functions. Its dis-regulation in the kidney leads to or is associated with certain renal diseases or disorders, most notably the urinary concentration defect. Hypertonicity, which the kidney medulla is normally exposed to, activates NFAT5 through phosphorylation of a signaling molecule or NFAT5 itself. Hypotonicity inhibits NFAT5 through a similar mechanism. More than a dozen of protein and lipid kinases have been identified to contribute to tonicity-dependent regulation of NFAT5. Hypertonicity activates NFAT5 by increasing its nuclear localization and transactivating activity in the early phase and protein abundance in the late phase. The known mechanism for inhibition of NFAT5 by hypotonicity is a decrease of nuclear NFAT5. The present article reviews the effect of each kinase on NFAT5 nuclear localization, transactivation and protein abundance, and the relationship among these kinases, if known. Cyclosporine A and tacrolimus suppress immune reactions by inhibiting the phosphatase calcineurin-dependent activation of NFAT1. It is hoped that this review would stimulate the interest to seek explanations from the NFAT5 regulatory pathways for certain clinical presentations and to explore novel therapeutic approaches based on the pathways. On the basic science front, this review raises two interesting questions. The first one is how these kinases can specifically signal to NFAT5 in the context of hypertonicity or hypotonicity, because they also regulate other cellular activities and even opposite activities in some cases. The second one is why these many kinases, some of which might have redundant functions, are needed to regulate NFAT5 activity. This review reiterates the concept of signaling through cooperation. Cells need these kinases working in a coordinated way to provide the signaling specificity that is lacking in the individual one. Redundancy in regulation of NFAT5 is a critical strategy for cells to maintain robustness against hypertonic or hypotonic stress. Core tip: NFAT5 is critical for kidney functions. Its disregulation results in or is associated with the renal diseases and disorders. More than a dozen of kinases have been identified to contribute to tonicity-dependent regulation of NFAT5. The present review is focused on how these kinases regulate NFAT5 activity under the context of hypertonicity or hypotonicity. Understanding these regulatory mechanisms will have therapeutic implications. A precedent example is that recognition of the cyclosporine immunosuppressive effect resulted from inhibition of the phosphatase calcineurin-dependent activation of NFAT1 allows combination use of cyclosporine with other mechanistically different immunosuppressants to improve their therapeutic efficacy and reduce their side effects.Zhou X. How do kinases contribute to tonicity-dependent regulation of the transcription factor NFAT5? World J Nephrol 2016; 5(1): 20-32 Available from:

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Biological functions of casein kinase 1 isoforms and putative roles in tumorigenesis

Cited by 196 publications

References 106 publications

The Role of Casein Kinase 1 in Meiosis

The Role of Casein Kinase 1 in Meiosis

HIF-2α phosphorylation by CK1δ promotes erythropoietin secretion in liver cancer cells under hypoxia

How do kinases contribute to tonicity-dependent regulation of the transcription factor NFAT5?

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