Cyclin H is a new binding partner for protein kinase CK2

Faust, Michael; Kartarius, Sabine; Schwindling, Sandra L; Montenarh, Mathias

doi:10.1016/s0006-291x(02)00825-2

Cited by 9 publications

(13 citation statements)

References 46 publications

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“…Moreover, in addition to being a binding partner, hPrp3p is also a substrate for the CK2 holoenzyme consisting of two regulatory and two catalytic a-or a 0 subunits, but not for the catalytic subunits alone. Binding partners for the individual subunits of CK2 were already detected earlier including hsp90, PP2a, Pim-1, CKIP-1, cyclin H, NAP1 and Egr-1 (Jain et al, 1996;Li et al, 1999;Bosc et al, 2000;Faust et al, 2002;Messenger et al, 2002). Some of these binding partners are also substrates for the CK2 kinase.…”

Section: Discussionmentioning

confidence: 83%

“…Among the more than 300 substrates discovered to this date, are a lot of proteins that are implicated in cell cycle control, DNA replication/repair, proliferation and transcription/translation (Meggio and Pinna, 2003). The C-terminal domain (CTD) of the largest RNA polymerase II subunit (Cabrejos et al, 2004), the TFIIF-dependent CTD phosphatase 1 (FCP1) (Palancade et al, 2002) and cyclin H (Faust et al, 2002;Schneider et al, 2002;Krempler et al, 2005) belong to the substrates that are known to regulate transcriptional events. Cyclin H is phosphorylated at threonine 315 by CK2 and this phosphorylation is needed for full activity of the cdk7/ cyclin H/Mat1 complex towards a CTD peptide of RNA polymerase II.…”

Section: Introductionmentioning

confidence: 99%

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Protein kinase CK2 interacts with the splicing factor hPrp3p

et al. 2007

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Numerous signalling pathways in cells are influenced by the ubiquitous Ser/Thr protein kinase CK2. Protein kinase CK2 is composed of two regulatory b-subunits and two catalytic a-or a 0 -subunits. Several of the known CK2 substrates are proteins known to regulate transcriptional events. Here, we describe that protein kinase CK2 interacts with the splicing factor hPrp3p, which is important for the assembly of the spliceosome. In a twohybrid screen hPrp3p is exclusively bound to the catalytic a-or a 0 -subunits of CK2 but not to the regulatory bsubunit. The interaction was confirmed by coimmunoprecipitation experiments in vitro and in vivo. Moreover, both proteins colocalized in nuclear speckles which is typical for splicing factor compartments within the nucleus. Phosphorylation experiments revealed that hPrp3p is also a substrate of protein kinase CK2. The main phosphorylation site was mapped to C-terminal residues. In vitro and in vivo splicing assays showed that the splicing activity is significantly influenced by the CK2-hPrp3p interaction. Thus, these data showed that CK2 is involved in the regulation of RNA processing.

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Section: Discussionmentioning

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Protein kinase CK2 interacts with the splicing factor hPrp3p

et al. 2007

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“…This master regulator of cell cycle progression is itself regulated by CK2. In this respect, the CK2a subunit forms a complex with and phosphorylates Cyclin H at serine 315 [27,28]. This phosphorylation event has no effect on CAK complex formation, but is critical for full CAK activity [28].…”

Section: Ck2 In the Cell Cyclementioning

confidence: 99%

Protein Kinase CK2 in Health and Disease

St‐Denis

Litchfield

2009

Cell. Mol. Life Sci.

252

102

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Protein kinase CK2 is a serine/threonine kinase with a multitude of protein substrates. The enzyme is ubiquitously expressed in mammalian cells, where it functions in a variety of cellular processes, including cell cycle progression, apoptosis, transcription, and viral infection. While the importance of CK2 in the mammalian life cycle is undisputed, the regulatory mechanisms coordinating its numerous functions remain elusive. In this review, we focus on the various roles of CK2 in the mammalian cell, with particular attention on its functions through the stages of the cell cycle and during the decision to undergo cell death. We highlight how these roles are controlled in part through direct transcriptional regulation by CK2, and how the constitutive activity of CK2 can be hijacked in the case of viral infection. Finally, we discuss possible ways in which these functions are integrated to allow the cell to respond appropriately in the presence of multiple signals.

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“…The consensus sequence contains serine or threonine residues surrounded by acidic amino acids [17]. This kinase is involved in various cellular processes, including proliferation, differentiation, apoptosis and angiogenesis [18][19][20][21]. However, the specific function of CK2 on leukocyte-endothelial cell interaction during TNF-α-induced inflammation remains elusive.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of protein kinase CK2 suppresses tumor necrosis factor (TNF)-α-induced leukocyte–endothelial cell interaction

Ampofo

Rudzitis‐Auth

Dahmke

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Inflammatory endothelial processes are regulated by the nuclear factor-κB (NF-κB) pathway, which involves phosphorylation of p65. Because p65 is a substrate of CK2, we herein investigated, whether this pleiotropic protein kinase may be a beneficial anti-inflammatory target. For this purpose, we analyzed in human dermal microvascular endothelial cells (HDMEC) the effect of CK2 inhibition by quinalizarin and CX-4945 on cell viability, adhesion molecule expression and NF-κB pathway activation. Leukocyte binding to HDMEC was assessed in an in vitro adhesion assay. Dorsal skinfold chambers in BALB/c mice were used to study leukocyte-endothelial cell interaction and leukocyte transmigration by means of repetitive intravital fluorescence microscopy and immunohistochemistry. We found that quinalizarin and CX-4945 effectively suppressed the activity of CK2 in HDMEC without affecting their viability. This was associated with a significant down-regulation of tumor necrosis factor (TNF)-α-induced E-selectin, intercellular adhesion molecule (ICAM)-1 and vascular cell adhesion molecule (VCAM)-1 expression due to a reduction of shuttling, phosphorylation and transcriptional activity of the NF-κB complex. In consequence, leukocyte binding to quinalizarin- and CX-4945-treated HDMEC was diminished. Finally, CX-4945 treatment significantly decreased the numbers of adherent and transmigrated leukocytes in dorsal skinfold chambers exposed to TNF-α in vivo. These findings indicate that CK2 is a key regulator of leukocyte-endothelial cell interaction in inflammation by regulating the expression of E-selectin, ICAM-1 and VCAM-1 via affecting the transcriptional activity of the NF-κB complex. Accordingly, CK2 represents a promising target for the development of novel anti-inflammatory drugs.

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Cyclin H is a new binding partner for protein kinase CK2

Cited by 9 publications

References 46 publications

Protein kinase CK2 interacts with the splicing factor hPrp3p

Protein kinase CK2 interacts with the splicing factor hPrp3p

Protein Kinase CK2 in Health and Disease

Inhibition of protein kinase CK2 suppresses tumor necrosis factor (TNF)-α-induced leukocyte–endothelial cell interaction

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