The HP1 protein family: getting a grip on chromatin

Eissenberg, Joel C.; Elgin, Sarah C. R.

doi:10.1016/s0959-437x(00)00058-7

Cited by 447 publications

(395 citation statements)

References 58 publications

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“…Nevertheless, these data suggest that the centro- mere clustering might be associated with alterations of higher-order chromatin structures that exceed the extent required for a simple remodeling in response to a decreased number of chromocenters. Potential regulators of these processes are Ikaros (16) and HP1 (47).…”

Section: Discussionmentioning

confidence: 99%

Spatial distribution patterns of interphase centromeres during retinoic acid‐induced differentiation of promyelocytic leukemia cells

et al. 2002

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Background:The pericentromeric heterochromatin is an important element for the regulation of gene silencing. Its spatial distribution during interphase appears to be celltype specific. This study analyzes three-dimensional (3D) centromere distribution patterns during cellular differentiation along the neutrophil pathway. Methods: Differentiation of the promyelocytic leukemia cell line NB4 was induced by retinoic acid. Centromeres in interphase nuclei were visualized by immunofluorescence staining of centromere-associated proteins with CREST serum. 3D images of nuclei were obtained by confocal microscopy. Automated methods for the segmentation of point-like objects in 3D images were implemented to detect the position of centromeres. Features of centromere localization patterns were determined by constructing the minimal spanning tree of the centromere distribution.

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Section: Discussionmentioning

confidence: 99%

Spatial distribution patterns of interphase centromeres during retinoic acid‐induced differentiation of promyelocytic leukemia cells

et al. 2002

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“…Lys9 methylation on H3 histone has been shown to recruit the heterochromatin-associated protein HP1, which plays a crucial role in maintaining the compact heterochromatic structure at centromeres (Eissenberg and Elgin, 2000). Recently, long-term TSA treatments in mouse cells have been reported to disrupt interphase nuclear domains enriched in HP1 proteins (Taddei et al, 2001).…”

Section: Centromeric Heterochromatin Is Modified When Histone Deacetymentioning

confidence: 99%

Histone Hyperacetylation in Mitosis Prevents Sister Chromatid Separation and Produces Chromosome Segregation Defects

Cimini

Mattiuzzo

Torosantucci

et al. 2003

MBoC

169

160

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Posttranslational modifications of core histones contribute to driving changes in chromatin conformation and compaction. Herein, we investigated the role of histone deacetylation on the mitotic process by inhibiting histone deacetylases shortly before mitosis in human primary fibroblasts. Cells entering mitosis with hyperacetylated histones displayed altered chromatin conformation associated with decreased reactivity to the anti-Ser 10 phospho H3 antibody, increased recruitment of protein phosphatase 1-δ on mitotic chromosomes, and depletion of heterochromatin protein 1 from the centromeric heterochromatin. Inhibition of histone deacetylation before mitosis produced defective chromosome condensation and impaired mitotic progression in living cells, suggesting that improper chromosome condensation may induce mitotic checkpoint activation. In situ hybridization analysis on anaphase cells demonstrated the presence of chromatin bridges, which were caused by persisting cohesion along sister chromatid arms after centromere separation. Thus, the presence of hyperacetylated chromatin during mitosis impairs proper chromosome condensation during the pre-anaphase stages, resulting in poor sister chromatid resolution. Lagging chromosomes consisting of single or paired sisters were also induced by the presence of hyperacetylated histones, indicating that the less constrained centromeric organization associated with heterochromatin protein 1 depletion may promote the attachment of kinetochores to microtubules coming from both poles

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“…When almost all nuclei displayed ACC (8 h after Fasinduction), these proteins were essentially undetectable in the NMP fraction ( Figure 5, open circles). At that time, a further set of proteins was significantly decreased, including the chromatin-associated proteins LBP-p40, 36 hnRNP C1, E, K, U, 37 MCM2/3, 38 HP-1g, 39 in addition to nucleoporin p62, annexin IV, prohibitin and an abundant, but yet uncharacterized, motor protein ( Figure 5, Table 1). …”

Section: Decrease Of Nuclear Proteins During Accmentioning

confidence: 99%

Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation

et al. 2002

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The nuclear matrix (NM) is considered a proteinaceous scaffold spatially organizing the interphase nucleus, the integrity of which is affected during apoptosis. Caspasemediated degradation of NM proteins, such as nuclear lamins, precedes apoptotic chromatin condensation (ACC). Nevertheless, other NM proteins remain unaffected, which most likely maintain a remaining nuclear structure devoid of chromatin. We, therefore, screened various types of apoptotic cells for changes of the nuclear matrix proteome during the process of apoptotic ACC. Expectedly, we observed fundamental alterations of known chromatin-associated proteins, comprising both degradation and translocation to the cytosol. Importantly, a consistent set of abundant NM proteins, some (e.g. hNMP 200) of which displaying structural features, remained unaffected during apoptosis and might therefore represent constituents of an elementary scaffold. In addition, proteins involved in DNA replication and DNA repair were found accumulated in the NM fraction before cells became irreversibly committed to ACC, a time point characterized in detail by inhibitor studies with orthovanadate. In general, protein alterations of a consistent set of NM proteins (67 of which were identified), were reproducibly detectable in Fasinduced Jurkat cells, in UV-light treated U937 cells and also in staurosporine-treated HeLa cells. Our data indicate that substantial alterations of proteins linking chromatin to an elementary nuclear protein scaffold might play an intriguing role for the process of ACC.

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The HP1 protein family: getting a grip on chromatin

Cited by 447 publications

References 58 publications

Spatial distribution patterns of interphase centromeres during retinoic acid‐induced differentiation of promyelocytic leukemia cells

Spatial distribution patterns of interphase centromeres during retinoic acid‐induced differentiation of promyelocytic leukemia cells

Histone Hyperacetylation in Mitosis Prevents Sister Chromatid Separation and Produces Chromosome Segregation Defects

Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation

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