The perichromosomal layer

Hooser, Aaron A. Van; Yuh, Patrick; Heald, Rebecca

doi:10.1007/s00412-005-0021-9

Cited by 100 publications

(105 citation statements)

References 94 publications

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“…We presume that Ki67 might contribute to the quality of mitosis as a hidden "safeguard" whose significance might be concealed even in Ki67-depleted cells until sensitized by depleting/inactivating the redundant molecules. At the periphery of each mitotic chromosome there is a specialized chromosome domain referred to as the perichromosomal layer (39,40). This layer is visible by electron microscopy (41) and its constituents, including Ki67, can be isolated together with the chromosomes (39).…”

Section: Discussionmentioning

confidence: 99%

“…At the periphery of each mitotic chromosome there is a specialized chromosome domain referred to as the perichromosomal layer (39,40). This layer is visible by electron microscopy (41) and its constituents, including Ki67, can be isolated together with the chromosomes (39). The particular function of this layer in the progression of mitosis has been discussed (39, 40) but not identified.…”

Section: Discussionmentioning

confidence: 99%

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Ki67 Antigen Contributes to the Timely Accumulation of Protein Phosphatase 1γ on Anaphase Chromosomes

Takagi

Nishiyama

Taguchi

et al. 2014

Journal of Biological Chemistry

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Background: Ki67 is a widely used cell proliferation marker whose cellular functions, however, remain elusive. Results: Ki67 interacts with protein phosphatase 1␥ (PP1␥) and modulates its localization in anaphase. Conclusion: Ki67 is a novel regulator of PP1␥ localization. Significance: This study shows a novel example of spatial and temporal control of dephosphorylation events on anaphase chromosomes.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Ki67 Antigen Contributes to the Timely Accumulation of Protein Phosphatase 1γ on Anaphase Chromosomes

Takagi

Nishiyama

Taguchi

et al. 2014

Journal of Biological Chemistry

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“…dRrp6 localizes to a large number of foci that are often arranged along the astral microtubules (MTs) and the cell cortex. At prometaphase, dRrp6 is detected on the condensed chromosomes and infrequently enveloping the chromosomes on the presumptive perichromosomal layer (PCL), a ribonucleoprotein structure that sheaths the chromosomes during mitosis (Van Hooser et al, 2005). In metaphase, dRrp6 localizes to either the spindle and PCL or, in a nonoverlapping manner, to the condensing chromosomes.…”

Section: Dynamic Chromosomal Association Of Drrp6 During Mitosismentioning

confidence: 99%

“…There are numerous RNA substrates during mitosis that could be candidate Rrp6 targets. For example, ribosomal RNAs associate with the PCL (Van Hooser et al, 2005). Many mRNAs and rRNAs reside on asters and spindles, where they are required for assembly of these structures in Xenopus cell-free extracts (Blower et al, 2005).…”

Section: Models For Rrp6 Function In Cell Cycle Progressionmentioning

confidence: 99%

Core Exosome-independent Roles for Rrp6 in Cell Cycle Progression

Graham

Kiss²,

Andrulis

2009

MBoC

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Exosome complexes are 3 to 5 exoribonucleases composed of subunits that are critical for numerous distinct RNA metabolic (ribonucleometabolic) pathways. Several studies have implicated the exosome subunits Rrp6 and Dis3 in chromosome segregation and cell division but the functional relevance of these findings remains unclear. Here, we report that, in Drosophila melanogaster S2 tissue culture cells, dRrp6 is required for cell proliferation and error-free mitosis, but the core exosome subunit Rrp40 is not. Micorarray analysis of dRrp6-depleted cell reveals increased levels of cell cycleand mitosis-related transcripts. Depletion of dRrp6 elicits a decrease in the frequency of mitotic cells and in the mitotic marker phospho-histone H3 (pH3), with a concomitant increase in defects in chromosome congression, separation, and segregation. Endogenous dRrp6 dynamically redistributes during mitosis, accumulating predominantly but not exclusively on the condensed chromosomes. In contrast, core subunits localize predominantly to MTs throughout cell division. Finally, dRrp6-depleted cells treated with microtubule poisons exhibit normal kinetochore recruitment of the spindle assembly checkpoint protein BubR1 without restoring pH3 levels, suggesting that these cells undergo premature chromosome condensation. Collectively, these data support the idea that dRrp6 has a core exosome-independent role in cell cycle and mitotic progression. INTRODUCTIONExosome complexes are critical players in the processing and degradation of many RNA species (Houseley et al., 2006). Found in both archaebacteria and eukaryotes, these complexes are composed of a "core" set of subunits. With respect to the yeast and human core complexes, they consist of six RNase PH domain-containing proteins (Rrp41, Rrp42, Rrp43, Rrp45, Rrp46, and Mtr3) and three S1 domain-containing proteins (Rrp4, Rrp40, and Csl4). Our understanding of exosome complex form and function has advanced greatly though the report of the crystal structures of archaebacterial (Buttner et al., 2005; and eukaryotic exosome core (Liu et al., 2006) complexes. The RNase PH subunits assemble into a hexameric ring upon which the S1 domain subunits reside. It has been proposed that the cylindrical shape and central channel of exosome complexes have evolved as a means to tightly regulate RNA recognition and subsequent decay (Lorentzen and Conti, 2006).Eukaryotes have compartment-specific exosome subunits and cofactors in addition to the core subunits. Although the eubacterial RNase R homolog Dis3 (also referred to as Rrp44) interacts with the yeast core (Mitchell et al., 1997;Allmang et al., 1999b;Dziembowski et al., 2007), it does not associate with either the human or trypanosome core (Chen et al., 2001;Estevez et al., 2003). Moreover, many archaebacteria lack an RNase R-like protein (Koonin et al., 2001). Thus, strictly speaking, Dis3 is not a core exosome component. Another exosome subunit missing in archaebacteria but present in eukaryotes is Rrp6, an RNase D homolog. Rrp6 associates specifical...

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“…The layer, designated the 'chromosome periphery' (HernandezVerdun and Gautier, 1994), appears at prometaphase and disappears at telophase during mitosis. It contains numerous components, including nuclear and nucleolar proteins as well as several RNAs (Van Hooser et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Nucleolin functions in nucleolus formation and chromosome congression

Matsunaga

Takata

et al. 2007

Journal of Cell Science

123

124

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A complex structure, designated the chromosome periphery, surrounds each chromosome during mitosis. Although several proteins have been shown to localize to the chromosome periphery, their functions during mitosis remain unclear. Here, we used a combination of highresolution microscopy and RNA-interference-mediated depletion to study the functions of nucleolin, a nucleolar protein localized at the chromosome periphery, in interphase and mitosis. During mitosis, nucleolin was localized in the peripheral region including the vicinity of the outer kinetochore of chromosomes. Staining with an antibody specific for nucleolin phosphorylated by CDC2 revealed that nucleolin was also associated with the spindle poles from prometaphase to anaphase. Nucleolin depletion resulted in disorganization of the nucleoli at interphase. Furthermore, nucleolin-depleted cells showed a prolonged cell cycle with misaligned chromosomes and defects in spindle organization. The misaligned chromosomes showed syntelic kinetochore-microtubule attachments with reduced centromere stretching. Taken together, our results indicate that nucleolin is required for nucleolus formation, and is also involved in chromosome congression and spindle formation. Journal of Cell Science 2092Nucleolin is an abundant nucleolar protein localized in the DFCs and GCs of nucleoli (Biqqioqera et al., 1990). Nucleolin plays essential roles in rDNA transcription, rRNA maturation, ribosome assembly and nucleocytoplasmic transport (Ginisty et al., 1999;Srivastava and Pollard, 1999). As a multifunctional protein, nucleolin has also been proposed to be a nuclear matrix-binding protein (Gotzmann et al., 1997), to interact with telomerase (Khurts et al., 2004) and to be involved in the regulation of apoptosis (Mi et al., 2003), intestinal cell differentiation (Turck et al., 2006) and remodeling of nucleosomes (Angelov et al., 2006). Although many functions of nucleolin have been clarified, previous studies have fallen short of demonstrating its functions during mitosis.Nucleolin is highly phosphorylated (Olson et al., 1975;Rao et al., 1982) and its phosphorylation is highly regulated during the cell cycle (Peter et al., 1990;Morimoto et al., 2005). Extensive phosphorylation by casein kinase 2 (CK2) occurs at interphase and by CDC2 during mitosis (Peter et al., 1990), and this regulated phosphorylation of nucleolin probably regulates nucleolin functions during the cell cycle (Ginisty et al., 1999). It has been demonstrated that phosphorylation of nucleolin at interphase is correlated with active rRNA transcription (Suzuki et al., 1987). Despite a previous study describing the localization of nucleolin phosphorylated by CDC2 (Dranovsky et al., 2001), no information about its functions during mitosis has been obtained to date.Here, we demonstrate that nucleolin localizes to the nucleoli, which are located in the peripheral region including the vicinity of the outer kinetochore of chromosomes, in interphase nuclei and during mitosis. Staining with an antibody specific for nucle...

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The perichromosomal layer

Cited by 100 publications

References 94 publications

Ki67 Antigen Contributes to the Timely Accumulation of Protein Phosphatase 1γ on Anaphase Chromosomes

Ki67 Antigen Contributes to the Timely Accumulation of Protein Phosphatase 1γ on Anaphase Chromosomes

Core Exosome-independent Roles for Rrp6 in Cell Cycle Progression

Nucleolin functions in nucleolus formation and chromosome congression

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