Interrelationships of nuclear structure and transcriptional control: Functional consequences of being in the right place at the right time

Stein, Gary S.; Wijnen, André J. van; Stein, Janet L.; Lian, Jane B.; Pockwinse, Shirwin M.; McNeil, Sandra

doi:10.1002/(sici)1097-4644(19980801)70:2<200::aid-jcb6>3.0.co;2-s

Cited by 39 publications

(6 citation statements)

References 73 publications

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“…Thus, even though CK2 appears to be generally unregulated in terms of its total activity, this and several other studies support the notion that its spatio‐temporal status in specific loci may be a key means of its functional regulation [Ahmed, 1999; Ahmed et al, 2000; Faust and Montenarh, 2000; Martel et al, 2001; Yu et al, 2001]. Of note, similar modes of regulation of signaling molecules in other systems have been recognized [Stein et al, 1998; Haj et al, 2002; Zaccolo and Pozzan, 2002].…”

Section: Discussionsupporting

confidence: 67%

“…Much recent evidence supports the notion that within the nucleus, distinct domains are present which may serve as targets for specific signals [for a review see Stein et al, 1998, 2000]. Considering the nuclear matrix as a key locus for CK2 nuclear signaling [for reviews see Tawfic et al, 1996, 2001; Ahmed, 1999, 2000], we reasoned that even though changes in CK2 in various phases of cell cycle were not apparent when measured as total activity, they might be reflected as discrete dynamic modulations at the level of the nuclear matrix.…”

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confidence: 93%

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Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix

Wang

Davis

et al. 2002

J of Cellular Biochemistry

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Protein kinase CK2 is a ubiquitous protein serine/threonine kinase that is involved in cell growth and proliferation as well as suppression of apoptosis. Several studies have suggested that the kinase plays a role in cell cycle progression; however, changes in enzyme activity during phases of cell cycle have not been detected. Nuclear matrix is a key locus for CK2 signaling in the nucleus. We therefore examined CK2 signaling to the nuclear matrix in distinct phases of cell cycle by employing synchronized ALVA-41 prostate cancer cells. Removal of serum from the culture medium resulted in G0/G1 arrest, and a reduction in the nuclear matrix-associated CK2 activity which was rapidly reversed on addition of serum. Arresting the cells in G(0)/G(1) phase with hydroxyurea and subsequent release to S phase by serum gave similar results. Cells arrested in the G(2)/M phase by treatment with nocodazole demonstrated an extensive reduction in the nuclear matrix-associated CK2 which was reversed rapidly on addition of serum. Changes in the immunoreactive CK2 protein were concordant with the activity data reflecting a dynamic trafficking of the kinase in distinct phases of cell cycle. Under the same conditions, CK2 activity in total cellular lysate remained essentially unaltered. These results provide the first direct evidence of discrete modulations of CK2 in the nuclear matrix during the cell cycle progression. Inducible overexpression of CK2 in CHO cells yielded only a modest increase in CK2 activity even though a significant increase in expression was apparent at the level of CK2 alpha-specific message. Stably transfected ALVA-41 cells, however, did not show a significant change in CK2 levels despite increased expression at the message level. Not surprisingly, both types of the stably transfected cells failed to show any alteration in cell cycle progression. Distribution of the CK2 activity in the cytosolic versus nuclear matrix fractions in normal cells appears to be different from that in the cancer cells such that the ratio of nuclear matrix to cytosolic activity is much higher in the latter. Considering that nuclear matrix is central to several nuclear functions, this pattern of intracellular distribution of CK2 may have implications for its role in the oncogenic process. Published 2003 Wiley-Liss, Inc.

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Section: Discussionsupporting

confidence: 67%

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confidence: 93%

Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix

Wang

Davis

et al. 2002

J of Cellular Biochemistry

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“…Accumulating evidence supports the idea that the nucleus is organized into higher-order structures comprising segregated domains of transcriptional and replicational activity (Wei et al 1998). However, this may not be restricted to the organization of the genome into chromosomal domains alone, but may extend to an underlying organization of the supporting nuclear architecture, which could be involved in the regulation of gene activity (Stein et al 1998). Based on these findings, we investigated whether YT bodies colocalize with sites of RNA synthesis using in situ BrUTP incorporation (Jackson et al 1993; Huang et al 1998).…”

Section: Resultsmentioning

confidence: 99%

The ER Repeat Protein Yt521-B Localizes to a Novel Subnuclear Compartment

Nayler

Hartmann

Stamm

2000

The Journal of Cell Biology

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The characterization of distinct subnuclear domains suggests a dynamic nuclear framework supporting gene expression and DNA replication. Here, we show that the glutamic acid/arginine-rich domain protein YT521-B localizes to a novel subnuclear structure, the YT bodies. YT bodies are dynamic compartments, which first appear at the beginning of S-phase in the cell cycle and disperse during mitosis. Furthermore, in untreated cells of the human cell line MCF7 they were undetectable and appeared only after drug- induced differentiation. YT bodies contain transcriptionally active sites and are in close contact to other subnuclear structures such as speckles and coiled bodies. YT bodies disperse upon actinomycin D treatment, whereas other transcriptional inhibitors such as α-amanitin or DRB have little effect. On the basis of our experiments, we propose that YT521-B may participate in the assembly of genes into transcription centers, thereby allowing efficient regulation of gene expression.

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“…Second, interactions between functional DNA/protein complexes and the nucleoskeleton have been found, such as in transcription or replication foci. These attachments are thought to be rather transient than permanent (Jackson and Cook 1985b, Jackson and Cook 1986; Hozák et al 1993; Hyrien et al 1997; Jackson 1997; Stein et al 1998).…”

mentioning

confidence: 99%

Intranuclear Anchoring of Repetitive DNA Sequences

Weipoltshammer

Schöfer

Almeder

et al. 1999

The Journal of Cell Biology

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Centromeres, telomeres, and ribosomal gene clusters consist of repetitive DNA sequences. To assess their contributions to the spatial organization of the interphase genome, their interactions with the nucleoskeleton were examined in quiescent and activated human lymphocytes. The nucleoskeletons were prepared using “physiological” conditions. The resulting structures were probed for specific DNA sequences of centromeres, telomeres, and ribosomal genes by in situ hybridization; the electroeluted DNA fractions were examined by blot hybridization. In both nonstimulated and stimulated lymphocytes, centromeric alpha-satellite repeats were almost exclusively found in the eluted fraction, while telomeric sequences remained attached to the nucleoskeleton. Ribosomal genes showed a transcription-dependent attachment pattern: in unstimulated lymphocytes, transcriptionally inactive ribosomal genes located outside the nucleolus were eluted completely. When comparing transcription unit and intergenic spacer, significantly more of the intergenic spacer was removed. In activated lymphocytes, considerable but similar amounts of both rDNA fragments were eluted. The results demonstrate that: (a) the various repetitive DNA sequences differ significantly in their intranuclear anchoring, (b) telomeric rather than centromeric DNA sequences form stable attachments to the nucleoskeleton, and (c) different attachment mechanisms might be responsible for the interaction of ribosomal genes with the nucleoskeleton.

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Interrelationships of nuclear structure and transcriptional control: Functional consequences of being in the right place at the right time

Cited by 39 publications

References 73 publications

Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix

Cell cycle dependent regulation of protein kinase CK2 signaling to the nuclear matrix

The ER Repeat Protein Yt521-B Localizes to a Novel Subnuclear Compartment

Intranuclear Anchoring of Repetitive DNA Sequences

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