Nucleolin (C23), a physiological substrate for casein kinase II

Schneider, Helge R.; Issinger, Olaf‐Georg

doi:10.1016/s0006-291x(88)80786-1

Cited by 36 publications

(20 citation statements)

References 16 publications

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“…CK2 is implicated in RNA splicing S Lehnert et al substrate of CK2 we used a C-terminal fragment of nucleolin (amino acids 269-710) (Schneider and Issinger, 1988). In this case we found an incorporation rate of 2 mol phosphate into 1 mol of the nucleolin fragment (not shown).…”

Section: Ck2βmentioning

confidence: 83%

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: Ck2βmentioning

confidence: 83%

Protein kinase CK2 interacts with the splicing factor hPrp3p

et al. 2007

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“…Activation of the MAP-kinases has been reported to be both intimin-dependent and -independent (44,48). Nucleolin is one target of several MAP-kinases, including p38 (49), extracellular-regulated kinase (50), and casein kinase 2 (51,52). Of particular note is the recent work of Savkovic et al (53) who showed that protein kinase C-is involved in EPEC-induced inflammatory responses of infected cells.…”

Section: Discussionmentioning

confidence: 99%

Intimin Types α, β, and γ Bind to Nucleolin with Equivalent Affinity but Lower Avidity than to the Translocated Intimin Receptor

Sinclair

O'Brien

2004

Journal of Biological Chemistry

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The outer membrane adhesins of enteropathogenic Escherichia coli, Citrobacter rodentium, and enterohemorrhagic E. coli (EHEC) O157:H7 that mediate attach and efface intestinal lesions are classified as intimin ␣, ␤, and ␥, respectively. Each of these intimin types binds to its cognate, bacterially encoded receptor (called Tir for translocated intimin receptor) to promote tight adherence of the organism to the host-cell plasma membrane. We previously reported that ␥ intimin of EHEC O157:H7 also bound to a eucaryotic receptor that we determined was nucleolin. The objective of this study was to investigate in vitro and in vivo the interactions of intimins ␣, ␤, and ␥ with nucleolin in the presence of Tir from EHEC O157:H7. Protein binding experiments demonstrated that intimin of types ␣, ␤, and ␥ bound nucleolin with similar affinity. Moreover, all three intimin types co-localized with regions of nucleolin expressed on the surface of HEp-2 cells. When intimin ␣, ␤, or ␥ bound to Tir in vitro, the intimin interaction with nucleolin was blocked. Both Tir and nucleolin accumulated beneath intimin-presenting bacteria that had attached to the surface of HEp-2 cells. Taken together, these findings suggest that nucleolin is involved in bacterial adherence promoted by all intimin types and that Tir and nucleolin compete for intimin during adherence.

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“…Myc and Myb (Luscher et al ., 1989(Luscher et al ., , 1990) SV40 large T antigen (Grisser et al ., 1988) Other Nucleolin (Schneider and Issinger, 1988) cAMP-regulated phosphoprotein (Girault et al ., 1989) for ATP and GTP as phosphate donors ; (c) inhibition by heparin; and (d) stimulation by polyamines (Thornburg et al ., 1979 ;Matthews and Huebner, 1984) . Nucleolus-associated CKII has been identified, has been shown to phosphorylate nucleolin as a substrate, and may be involved in ribosome assembly (Caizergues-Ferrer et al ., 1987 ;Schneider and Issinger, 1988) and regulation of rDNA transcription (Belenguer et al, 1989).…”

Section: Oncoproteinsmentioning

confidence: 99%

“…Nucleolus-associated CKII has been identified, has been shown to phosphorylate nucleolin as a substrate, and may be involved in ribosome assembly (Caizergues-Ferrer et al ., 1987 ;Schneider and Issinger, 1988) and regulation of rDNA transcription (Belenguer et al, 1989).…”

Section: Oncoproteinsmentioning

confidence: 99%

Immunocytochemical localization of casein kinase II during interphase and mitosis.

Spector

Bae

et al. 1991

The Journal of Cell Biology

119

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Abstract. We have developed specific antibodies to synthetic peptide antigens that react with the individual subunits of casein kinase 11 (CKII) . Using these antibodies, we studied the localization of CKII in asynchronous HeLa cells by immunofluorescence and immunoelectron microscopy. Further studies were done on HeLa cells arrested at the Gl/S transition by hydroxyurea treatment . Our results indicate that the CKII a and ß subunits are localized in the cytoplasm C ASEIN kinase II (CKII)' is a ubiquitous protein serlne/threonine kinase found in eukaryotic cells (Edelman et al . 1987 and highly conserved among eukaryotic organisms, including Drosophila, yeast, C. elegans, bovine, and human (Saxena et al ., 1987;Chen-Wu et al ., 1988;Hu and Rubin, 1990a ;Lozeman, 1990). Casein kinase II from several species share a common polypeptide subunit structure, a2ß2, with a of M 37,000-44,000 and ß of M 24,000-28,000 by electrophoresis (Edelman et al ., 1987) . Two forms of a are known designated a (M 41,000-44,000) and a' (M, 37,000-42,000) . The a and a' subunits are thought to be the catalytic subunits based on their kinase activity in the absence of the ß subunit and sequences common to other protein kinases (Hathaway et al ., 1981; Cochet and Chambaz, 1983 ;Chen-wu et al ., 1988 ;Meisner et al., 1989;. The function of the ß subunit is unknown, and it shares no extensive homology to other known protein sequences (Jakobi et al ., 1989) . The ß subunit has a high degree of polarity with clusters ofnegative charges in the amino-terminal region and positive charge clusters in the carboxy-terminal region (Takio et al., 1987) . The basic compounds, spermine, spermidine, and polylysine, stimulate activity by interacting at least in part with the ß subunit (Traugh et al ., 1990) . This subunit may have a regulatory role in the holoenzyme (Takio et al., 1987), and evidence supporting this has been found in A-431 cells (Ackerman et al ., 1990). The comparative studies using the native CKII holoenzyme and the bacterially expressed a subunit show that the expressed a is inhibited by heparin, but it is not stimulated by polyamines and has 9% of K t of the holoenzyme (Hu and Rubin, 1990b during interphase and are distributed throughout the cell during mitosis . Further electron microscopic investigation revealed that CKII a subunit is associated with spindle fibers during metaphase and anaphase. In contrast, the CKII a' subunit is localized in the nucleus during GI and in the cytoplasm during S. Taken together, our results suggest that CKII may play significant roles in cell division control by shifting its localization between the cytoplasm and nucleus .further suggests that CKII holoenzyme is stabilized by interaction with the ß subunit .

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Nucleolin (C23), a physiological substrate for casein kinase II

Cited by 36 publications

References 16 publications

Protein kinase CK2 interacts with the splicing factor hPrp3p

Protein kinase CK2 interacts with the splicing factor hPrp3p

Intimin Types α, β, and γ Bind to Nucleolin with Equivalent Affinity but Lower Avidity than to the Translocated Intimin Receptor

Immunocytochemical localization of casein kinase II during interphase and mitosis.

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