Protein kinase CK2 catalyzes tyrosine phosphorylation in mammalian cells

Vilk, Greg; Weber, Jane E.; Turowec, Jacob P.; Duncan, James S.; Wu, Chenggang; Derksen, David R.; Zień, Piotr; Sarno, Stefania; Donella‐Deana, Arianna; Lajoie, Gilles; Pinna, Lorenzo A.; Li, Shawn S.‐C.; Litchfield, David W.

doi:10.1016/j.cellsig.2008.07.002

Cited by 52 publications

(41 citation statements)

References 60 publications

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“…3b). The presence of these rare peptides does, however, suggest that some of the parasite's serine/threonine protein kinase/s possess dual specificity and are able to also phosphorylate tyrosine residues, as has been established in other ePKs, for example protein kinase CK2 31 . We are currently investigating this possibility.…”

Section: Resultsmentioning

confidence: 99%

Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum

et al. 2011

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The role of protein phosphorylation in the life cycle of malaria parasites is slowly emerging. Here we combine global phospho-proteomic analysis with kinome-wide reverse genetics to assess the importance of protein phosphorylation in Plasmodium falciparum asexual proliferation. We identify 1177 phosphorylation sites on 650 parasite proteins that are involved in a wide range of general cellular activities such as DnA synthesis, transcription and metabolism as well as key parasite processes such as invasion and cyto-adherence. several parasite protein kinases are themselves phosphorylated on putative regulatory residues, including tyrosines in the activation loop of PfGsK3 and PfCLK3; we show that phosphorylation of PfCLK3 Y526 is essential for full kinase activity. A kinome-wide reverse genetics strategy identified 36 parasite kinases as likely essential for erythrocytic schizogony. These studies not only reveal processes that are regulated by protein phosphorylation, but also define potential anti-malarial drug targets within the parasite kinome.

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Section: Resultsmentioning

confidence: 99%

Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum

et al. 2011

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“…We wished to use another approach first to confirm that Spt2 is a phosphoprotein in vivo and second to identify the Spt2 residues targeted for phosphorylation. Whereas CK2 has been shown to be a serine/threonine kinase in various organisms (26), several studies have indicated that in yeast, it can also function as a tyrosine kinase (27)(28)(29)(30). Therefore, we asked whether Spt2 is phosphorylated in vivo on serine or tyrosine residues.…”

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confidence: 99%

Casein Kinase 2 Associates with the Yeast Chromatin Reassembly Factor Spt2/Sin1 To Regulate Its Function in the Repression of Spurious Transcription

Bhat

Boutin

Rufiange

et al. 2013

Molecular and Cellular Biology

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Spt2/Sin1 is a DNA binding protein with HMG-like domains. It plays a role in chromatin modulations associated with transcription elongation in Saccharomyces cerevisiae. Spt2 maintains the nucleosome level in coding regions and is important for the inhibition of spurious transcription in yeast. In this work, we undertook a biochemical approach to identify Spt2-interacting partners. Interestingly, casein kinase 2 (CK2) interacts with Spt2 and phosphorylates it in vitro as well as in vivo on two small regions, region I (RI) (amino acids 226 to 230) and RII (amino acids 277 to 281), located in its essential C-terminal domain. Mutation of the phosphorylation sites in RI and RII to acidic residues, thereby mimicking CK2 phosphorylation, leads to the inhibition of Spt2 function in the repression of spurious transcription and to a loss of its recruitment to coding regions. Inversely, depleting cells of CK2 activity leads to an increased Spt2 association with genes. We further show that Spt2 physically interacts with the essential histone chaperone Spt6 and that this association is inhibited in vitro and in vivo by CK2-dependent phosphorylation. Taken together, our data suggest that CK2 regulates the function of Spt2 by modulating its interaction with chromatin and the histone chaperone Spt6.

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“…It's not clear how CK2 can trigger JAK2 activation. One possibility is that CK2, via its Ser/Thr or even Tyr kinase activity, 47 phosphoryates JAK2 at one or multiple sites that are essential for the activation of the tyrosine kinase activity of JAK2. Such possibility is…”

Section: Vs Lane 2)mentioning

confidence: 99%

Identification of a novel function of the clathrin-coated structure at the plasma membrane in facilitating GM-CSF receptor-mediated activation of JAK2

et al. 2012

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Protein kinase CK2 catalyzes tyrosine phosphorylation in mammalian cells

Cited by 52 publications

References 60 publications

Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum

Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum

Casein Kinase 2 Associates with the Yeast Chromatin Reassembly Factor Spt2/Sin1 To Regulate Its Function in the Repression of Spurious Transcription

Identification of a novel function of the clathrin-coated structure at the plasma membrane in facilitating GM-CSF receptor-mediated activation of JAK2

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