Protein Kinase CK2 in Health and Disease

Filhol, Odile; Cochet, Claude

doi:10.1007/s00018-009-9151-1

Cited by 114 publications

(54 citation statements)

References 79 publications

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“…We identified kinases or their accessory factors of seven PK systems, six of which have been implicated in nuclear roles in Plasmodium or other eukaryotes: PfMAT1 (PFE0610c) [88]; the α- and β-subunits of casein kinase 2 (PF11_0096, PF11_0048) [89-91]; casein kinase 1 (PF11_0377) [92,93]; the catalytic and regulatory subunits of cAMP-dependent protein kinase (PFI1685w, PFL1110c) [94]; NIMA-related protein kinase PfNEK-1 (PFL1370w) [95,96]; and mitogen-activated protein kinase 2 PfMAP2 (PF11_0147) [97,98]. PfMAP2 is a substrate of PfNEK-1 [96] and both kinases are essential for completion of the IDC in P. falciparum [95,99], whereas in P. berghei PbMAP2 is implicated specifically in the development of male gametes [97].…”

Section: Discussionmentioning

confidence: 99%

Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum

et al. 2012

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BackgroundThe post-genomic era of malaria research provided unprecedented insights into the biology of Plasmodium parasites. Due to the large evolutionary distance to model eukaryotes, however, we lack a profound understanding of many processes in Plasmodium biology. One example is the cell nucleus, which controls the parasite genome in a development- and cell cycle-specific manner through mostly unknown mechanisms. To study this important organelle in detail, we conducted an integrative analysis of the P. falciparum nuclear proteome.ResultsWe combined high accuracy mass spectrometry and bioinformatic approaches to present for the first time an experimentally determined core nuclear proteome for P. falciparum. Besides a large number of factors implicated in known nuclear processes, one-third of all detected proteins carry no functional annotation, including many phylum- or genus-specific factors. Importantly, extensive experimental validation using 30 transgenic cell lines confirmed the high specificity of this inventory, and revealed distinct nuclear localization patterns of hitherto uncharacterized proteins. Further, our detailed analysis identified novel protein domains potentially implicated in gene transcription pathways, and sheds important new light on nuclear compartments and processes including regulatory complexes, the nucleolus, nuclear pores, and nuclear import pathways.ConclusionOur study provides comprehensive new insight into the biology of the Plasmodium nucleus and will serve as an important platform for dissecting general and parasite-specific nuclear processes in malaria parasites. Moreover, as the first nuclear proteome characterized in any protist organism, it will provide an important resource for studying evolutionary aspects of nuclear biology.

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Section: Discussionmentioning

confidence: 99%

Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum

et al. 2012

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“…Pronounced nuclear or nucleolar localization of CK2 subunits was observed in vertebrate cells. In the nucleolus, CK2 participates in rRNA transcription by phosphorylating different components of the RNA polymerase I transcription machinery (44,45). Proteins involved in ribosome biogenesis, such as B23 (also known as nucleophosmin), are also CK2 phosphorylation targets.…”

Section: Discussionmentioning

confidence: 99%

“…The CK2 holoenzyme is a heterotetramer composed of two regulatory ␤-subunits and two catalytic ␣-subunits; however, independent functions of both subunits have also been described. CK2-mediated phosphorylation controls the activity, localization, stability, or interactions of a multitude of substrate proteins found in different cellular compartments (44,45). Further complexity arises by the presence of several CK2␤ isoforms in Drosophila (46).…”

Section: ) (C and D)mentioning

confidence: 99%

Drosophila Mbm Is a Nucleolar Myc and Casein Kinase 2 Target Required for Ribosome Biogenesis and Cell Growth of Central Brain Neuroblasts

Hovhanyan

Herter

Pfannstiel

et al. 2014

Molecular and Cellular Biology

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“…(38) How, why and where the CK2 subunits will interact is still under investigation. (39) In THP-1 cells, the regulatory and catalytic subunits of CK2…”

Section: Ck2 Subunits and Fadd Colocalize Into The Nucleusmentioning

confidence: 99%

“…The fact that colocalization of FADD and CK2 was restricted to the nucleus is of significance since a large number of CK2 substrates are found in the nucleus and many of these are usually DNA/RNA structural proteins and transcription factors. (39) It is known that nuclear CK2 is correlated with apoptosis resistance which might be reminiscent of a potential role of CK2 in FADD antiapoptotic activities. (29) We found that in condition where TBB is added to THP-1 cells, the latter showed a higher sensitivity to cell death (unpublished).…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Modulatory role of the anti-apoptotic protein kinase CK2 in the sub-cellular localization of Fas associated death domain protein (FADD)

Vilmont

Filhol

Hesse

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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The Fas associated death domain protein (FADD) is the key adaptor molecule of the apoptotic signal triggered by death receptors of the TNF-R1 superfamily. Besides its crucial role in the apoptotic machinery, FADD has proved to be important in many biological processes like tumorigenesis, embryonic development or cell cycle progression. In a process to decipher the regulatory mechanisms underlying FADD regulation, we identified the anti-apoptotic kinase, CK2, as a new partner and regulator of FADD sub-cellular localization. The blockade of CK2 activity induced FADD re-localization within the cell. Moreover, cytoplasmic FADD was increased when CK2β was knocked down. In vitro kinase and pull down assays confirmed that FADD could be phosphorylated by the CK2 holoenzyme. We found that phosphorylation is weak with CK2α alone and optimal in the presence of stoichiometric amounts of CK2α catalytic and CK2β regulatory subunit, showing that FADD phosphorylation is undertaken by the CK2 holoenzyme in a CK2β-driven fashion. We found that CK2 can phosphorylate FADD on the serine 200 and that this phosphorylation is important for nuclear localization of FADD. Altogether, our results show for the first time that multifaceted kinase, CK2, phosphorylates FADD and is involved in its sub-cellular localization. This work uncovered an important role of CK2 in stable FADD nuclear localization.

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Protein Kinase CK2 in Health and Disease

Cited by 114 publications

References 79 publications

Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum

Organellar proteomics reveals hundreds of novel nuclear proteins in the malaria parasite Plasmodium falciparum

Drosophila Mbm Is a Nucleolar Myc and Casein Kinase 2 Target Required for Ribosome Biogenesis and Cell Growth of Central Brain Neuroblasts

Modulatory role of the anti-apoptotic protein kinase CK2 in the sub-cellular localization of Fas associated death domain protein (FADD)

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