Growth-dependent modulation of casein kinase II and its substrate nucleolin in primary human cell cultures and HeLa cells

Schneider, Helge R.; Issinger, Olaf‐Georg

doi:10.1016/0167-4889(89)90246-2

Cited by 19 publications

(9 citation statements)

References 12 publications

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“…Nucleolin is phosphorylated on serine residues by casein kinase 2 (CK2) (38, 39) during interphase, suggesting phosphorylation plays a role in the control of rDNA transcription, but nucleolin is phosphorylated on threonine residues by cdc2 kinase during mitosis, which has been linked to mitotic reorganization of nucleolar chromatin (40,41). CK2 activity increases during cellular growth and declines when cells reach quiescence in parallel with the phosphorylation status of nucleolin (42) suggesting that CK2 may be an upstream effector of nucleolin. This idea is strengthened by the fact that the ␣-subunit of CK2 is physically associated with nucleolin (43).…”

Section: Resultsmentioning

confidence: 99%

Up-regulation of Nucleolin mRNA and Protein in Peripheral Blood Mononuclear Cells by Extracellular-regulated Kinase

Westmark

Malter

2001

Journal of Biological Chemistry

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The signal transduction pathways regulating nucleolin mRNA and protein production have yet to be elucidated. Peripheral blood mononuclear cells treated with phorbol 12-myristate 13-acetate showed steady state levels of nucleolin mRNA that were 2-2.5-fold greater than untreated control cells. The up-regulation of nucleolin mRNA was substantially repressed by U0126, a specific inhibitor that blocks phosphorylation of extracellularregulated kinase (ERK). Calcium ionophores A23187 and ionomycin also activated ERK and substantially elevated nucleolin mRNA levels, demonstrating phorbol 12-myristate 13-acetate and calcium signaling converge on ERK. Drugs that affected protein kinase C, protein kinase A, and phospholipase C signal transduction pathways did not alter nucleolin mRNA levels significantly. The half-life of nucleolin mRNA increased from 1.8 h in resting cells to 3.2 h with phorbol ester activation, suggesting ERK-mediated posttranscriptional regulation. Concomitantly, full-length nucleolin protein was increased. The higher levels of nucleolin protein were accompanied by increased binding of a 70-kDa nucleolin fragment to the 29-base instability element in the 3-untranslated region of amyloid precursor protein (APP) mRNA in gel mobility shift assays. Supplementation of rabbit reticulocyte lysate with nucleolin decreased APP mRNA stability and protein production. These data suggest ERK up-regulates nucleolin posttranscriptionally thereby controlling APP production.

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Section: Resultsmentioning

confidence: 99%

Up-regulation of Nucleolin mRNA and Protein in Peripheral Blood Mononuclear Cells by Extracellular-regulated Kinase

Westmark

Malter

2001

Journal of Biological Chemistry

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“…This activity was linked to nucleolin's influence on cell cycle progression, embryonic development and tumorigenesis. [103][104][105] The proteolytic cleavage of nucleolin into 30-and 72-kDa peptides was also enhanced by CKII. 106 PKC.…”

Section: Nucleolin and The Hallmarks Of Cancermentioning

confidence: 96%

RNA-binding protein nucleolin in disease

2012

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“…On the other hand, the phosphorylation of nucleolin was catalysed by casein kinase II in many tissues (Caizergues-Ferrer et al., 1987;Suzuki et al, 1987;Saito et al, 1988;Schneider and Issinger, 1988), and that the phosphorylation of nucleolin in 3T3-F442A cells enhanced its proteolytic degradation to 30 kDa and 72 kDa peptides (Warrener and Petryshyn,). The activities of casein kinase II and rRNA synthesis were found to be dependent on hormonal stimulus in hepatocytes (Suzuki et al, 1987) and lymphosarcoma P1798 (Suzuki et al, 1992) and on cell growth in HeLa cells (Schneider and Issinger, 1989). These facts raise the possibility that the phosphorylation of nucleolin and its preferential degradation to p60 or other smaller peptides may be something to do with pre-rRNA synthesis and maturation of rRNA.…”

Section: I1mentioning

confidence: 99%

Limited proteolysis of rat liver nucleolin by endogenous proteases: effects of polyamines and histones

Suzuki

Hosoya

1993

Biochemical Journal

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Nucleolin is a major nucleolar phosphoprotein and is presumably involved in rDNA transcription and ribosome biosynthesis. This protein is known to be very labile and to be cleaved by endogenous proteases into many small peptides. We found that, when rat liver nucleolar suspension (Nu-1) or nucleolin-rich extract (Nu-2) was incubated under conventional conditions, polyamines and histones interacted with the nucleolin to lead to its preferential degradation to 60 kDa phosphopeptide (p60). The peptide p60 was identified as a peptide containing the N-terminal half of the nucleolin molecule, as judged from peptide-map analysis. Whereas spermine binding to the purified nucleolin was decreased by KCl concentrations above 50 mM, histones (H1, H2B and H3) were able to bind to the nucleolin in the presence of up to 300 mM KCl. A distinct difference between H1 and other histones was found in that H1 could produce p60 from nucleolin in both Nu-1 and Nu-2, whereas H2B and H3 stimulated the degradation of nucleolin to p60 only when Nu-2 was used for the source of nucleolin. A possible relationship between p60 formation and rRNA synthesis is discussed, but its exact role remains to be studied.

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Growth-dependent modulation of casein kinase II and its substrate nucleolin in primary human cell cultures and HeLa cells

Cited by 19 publications

References 12 publications

Up-regulation of Nucleolin mRNA and Protein in Peripheral Blood Mononuclear Cells by Extracellular-regulated Kinase

Up-regulation of Nucleolin mRNA and Protein in Peripheral Blood Mononuclear Cells by Extracellular-regulated Kinase

RNA-binding protein nucleolin in disease

Limited proteolysis of rat liver nucleolin by endogenous proteases: effects of polyamines and histones

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