Casein kinase II induces c-fos expression via the serum response element pathway and p67SRF phosphorylation in living fibroblasts.

Gauthier-Rouvière, Cécile; Basset, M.; Blanchard, Jean Marie; Cavadore, Jean‐Claude; Fernandez, Anne; Lamb, Ned

doi:10.1002/j.1460-2075.1991.tb07842.x

Cited by 77 publications

(27 citation statements)

References 41 publications

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“…In contrast, nucleolin is constantly present in the nucleoli but highly phosphorylated in growing cells and dephosphorylated in confluent cells (23). ln line with these data, several authors described that CK2, or especially its ␤ subunit, was located mainly in the nucleus of growing cells but spread throughout cells that are serumstarved or confluent (16,17,40). Therefore, a coordinated spatiotemporal distribution of FGF-2 and CK2 in the nucleus could allow the regulation of specific nuclear protein phosphorylations, such as nucleolin phosphorylation during the G 1 /S transition.…”

Section: Figmentioning

confidence: 80%

“…Genetic studies showed that the kinase activity of CK2 is essential for viability of yeast (15). The involvement of CK2 in mitogenic signaling is strongly supported by approaches using microinjection of CK2 (16) or antibodies raised against CK2 (17,18). Moreover, several reports correlate an increase in CK2 activity with cell growth stimulation (reviewed in Ref.…”

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confidence: 99%

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Fibroblast Growth Factor-2 Binds to the Regulatory β Subunit of CK2 and Directly Stimulates CK2 Activity toward Nucleolin

Bonnet

Filhol

Truchet

et al. 1996

Journal of Biological Chemistry

144

115

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The presence of fibroblast growth factor-2 (FGF-2) in the nucleus has now been reported both in vitro and in vivo, but its nuclear functions are unknown. Here, we show that FGF-2 added to nuclear extract binds to protein kinase CK2 and nucleolin, a CK2 natural substrate. Added to baculovirus-infected cell extracts overexpressing CK2 or its isolated subunits, FGF-2 binds to the enzyme through its regulatory ␤ subunit. Using purified proteins, FGF-2 is shown to directly interact with CK2 and to stimulate CK2 activity toward nucleolin. Furthermore, a mitogenic-deficient FGF-2 mutant protein has an impaired ability to interact with CK2 and to stimulate CK2 activity using nucleolin as substrate. We propose that in growing cells, one function of nuclear FGF-2 is to modulate CK2 activity through binding to its regulatory ␤ subunit.The fibroblast growth factors (FGFs) 1 family includes nine polypeptides of which FGF-1 and FGF-2 (acidic and basic FGF) are prototype members (reviewed in Refs. 1 and 2). FGF-2 exerts its pleiotropic effects in cell growth and differentiation through a dual receptor system consisting of four different high-affinity transmembrane receptor tyrosine kinases and low-affinity binding sites corresponding to heparan sulfate proteoglycans (reviewed in Refs. 2 and 3). In addition, FGF-1 and FGF-2 are translocated from outside the cell to the nucleus (reviewed in Ref.2). Many other growth factors have been detected in the cell nucleus (reviewed in Refs. 4 and 5). In the case of Schwannomaderived growth factor and FGF-1, nuclear localization is necessary for mitogenic activity (6 -8). For FGF-2, nuclear translocation is correlated to cell proliferation, since it is no longer recovered in the nucleus of confluent cells (9, 10). Therefore, these data strongly suggest that FGF-2, as well as other growth factors, plays specific, but still unknown, nuclear functions in addition to classical signaling through cell surface receptors.We reported previously that in synchronized ABAE growing cells, a large increase of ribosomal genes transcription is tightly correlated to the nuclear translocation of FGF-2 and especially to an accumulation of the growth factor in the nucleolus. In contrast, in quiescent cells ribosomal genes transcription is 20-fold lower, and FGF-2 is exclusively found in the cytoplasm (9, 10). Upon addition of FGF-2 to nuclei of serum-starved cells, a 6-fold increase of ribosomal genes transcription is observed together with an increase in phosphorylation of nuclear proteins, essentially of nucleolin (9, 11); These data suggest that a nuclear function of FGF-2 could be to regulate ribosomal genes transcription by modulating the phosphorylation level of nuclear and nucleolar proteins as nucleolin. Nucleolin that is the major component of nucleolus is also a major substrate for protein kinase CK2 in rapidly proliferating tissues, and its phosphorylation level is correlated to the rate of ribosome biogenesis (reviewed in Ref. 12). CK2 is a serine/threonine protein kinase present in both the cyt...

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Section: Figmentioning

confidence: 80%

mentioning

confidence: 99%

Fibroblast Growth Factor-2 Binds to the Regulatory β Subunit of CK2 and Directly Stimulates CK2 Activity toward Nucleolin

Bonnet

Filhol

Truchet

et al. 1996

Journal of Biological Chemistry

144

115

View full text Add to dashboard Cite

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“…CKII activity has been reported to be induced by mitogenic stimulation in several systems (Sommercorn et al 1987;Karlund and Czech 1988;Ackerman and Osheroff 1989;Carroll and Marshak 1989), but this stimulation is relatively small (1.5-to 6-fold) and no concordant enhancement in the phosphorylation of a cellular substrate has been reported. On the other hand, the subcellular localization of CKII has recently been shown to differ though the cell cycle; in particular, the enzyme migrates out of the nucleus in S phase (Gauthier-Rouviere et al 1991;Yu et al 1991). This might suggest a model whereby Max DNA-binding activity that is present in quiescent cells is diminished following mitogenic stimulation by both CKII phosphorylation of Max and induction of Myc protein, and/or elevated in S phase when CKII activity in the nucleus is reduced and phosphatase PP2A activity rises ( Fig.…”

Section: Discussionmentioning

confidence: 99%

Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.

Berberich

Cole²

1992

Genes Dev.

214

112

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Max is a heterodimeric partner of the Myc oncoprotein with sequence-specific DNA-binding activity. We found that the DNA-binding activity of bacterially expressed Max homodimers was inhibited in an ATP-dependent reaction by phosphorylation in vitro with purified bovine casein kinase II (CKII). In contrast, phosphorylation of Max and/or Myc by CKII had no inhibitory or stimulatory effect on the DNA-binding activity of Myc/Max heterodimers. By deletion analysis and site-directed mutagenesis, the inhibitory domain was localized to a CKII phosphorylation site in the amino terminus of Max. Finally, extracts prepared from NIH-3T3 cell lines that overexpress Max contained a phosphorylated Max protein which, following phosphatase treatment or heterodimerization with Myc, was capable of sequence-specific DNA-binding activity. Immunoprecipitation experiments confirmed that Max was also phosphorylated in NIH-3T3 cells, demonstrating that Max phosphorylation may have an important physiological function.

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“…SRF is required for both the induction of immediate early genes by growth factors and the induction of muscle-specific genes during differentiation. Microinjection of anti-SRF antibodies blocked the serum induction of the c-fos gene in NIH3T3 cells as well as the expression of musclespecific genes and the terminal differentiation of C2C12 skeletal myoblasts (9,10).…”

mentioning

confidence: 97%

Megakaryoblastic Leukemia-1/2, a Transcriptional Co-activator of Serum Response Factor, Is Required for Skeletal Myogenic Differentiation

Selvaraj

Prywes

2003

Journal of Biological Chemistry

128

146

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Serum response factor (SRF) is required for the expression of a wide variety of muscle-specific genes that are expressed upon differentiation and is thus required for both striated and smooth muscle differentiation in addition to its role in regulating growth factor-inducible genes. A heart and smooth muscle-specific SRF co-activator, myocardin, has been shown to be required for cardiac development and smooth muscle differentiation. However, no such co-factors of SRF have been identified in the skeletal myogenic differentiation program. Myocardin and the related transcription factor megakaryoblastic leukemia-1 (MKL1/MAL/MRTF-A) can strongly potentiate the activity of SRF. Here we report the cloning of the third member of the myocardin/MKL family in humans, MKL2. MKL2 binds to and activates SRF similar to myocardin and MKL1. To determine the role of these factors in skeletal myogenic differentiation we used a dominant negative MKL2 to show that the MKL family of proteins is required for skeletal myogenic differentiation. Expression of the dominant negative protein in C2C12 skeletal myoblasts blocked the differentiation-induced expression of the SRF target genes skeletal ␣-actin and ␣-myosin heavy chain and blocked differentiation of the myoblasts to myotubes in vitro. C2C12 cells express both MKL1 and MKL2, but not myocardin, implicating MKL1 and/or MKL2 in the requirement for skeletal myogenic differentiation. MKL1 was predominantly cytoplasmic in C2C12 cells, with a small amount in the nucleus, however, no movement of MKL1 to the nucleus was observed upon differentiation.

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Casein kinase II induces c-fos expression via the serum response element pathway and p67SRF phosphorylation in living fibroblasts.

Cited by 77 publications

References 41 publications

Fibroblast Growth Factor-2 Binds to the Regulatory β Subunit of CK2 and Directly Stimulates CK2 Activity toward Nucleolin

Fibroblast Growth Factor-2 Binds to the Regulatory β Subunit of CK2 and Directly Stimulates CK2 Activity toward Nucleolin

Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers.

Megakaryoblastic Leukemia-1/2, a Transcriptional Co-activator of Serum Response Factor, Is Required for Skeletal Myogenic Differentiation

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