Dynamics of Nuclear Envelope Proteins During the Cell Cycle in Mammalian Cells

2002 ◽  
pp. 15-28 ◽  
Author(s):  
Jan Ellenberg
Keyword(s):  
Cell Cycle ◽  
Nuclear Envelope ◽  
Mammalian Cells ◽  
Envelope Proteins

scholarly journals Nesprin-2 Interacts with Condensin Component SMC2

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Xin Xing ◽  
Carmen Mroß ◽  
Linlin Hao ◽  
Martina Munck ◽  
Alexandra Herzog ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Nuclear Envelope ◽  
Envelope Proteins ◽  
S Phase ◽  
Nuclear Shape ◽  
The Core ◽  
Chromatin Interactions ◽  
Dividing Cells ◽  
Chromatin Bridges

The nuclear envelope proteins, Nesprins, have been primarily studied during interphase where they function in maintaining nuclear shape, size, and positioning. We analyze here the function of Nesprin-2 in chromatin interactions in interphase and dividing cells. We characterize a region in the rod domain of Nesprin-2 that is predicted as SMC domain (aa 1436–1766). We show that this domain can interact with itself. It furthermore has the capacity to bind to SMC2 and SMC4, the core subunits of condensin. The interaction was observed during all phases of the cell cycle; it was particularly strong during S phase and persisted also during mitosis. Nesprin-2 knockdown did not affect condensin distribution; however we noticed significantly higher numbers of chromatin bridges in Nesprin-2 knockdown cells in anaphase. Thus, Nesprin-2 may have an impact on chromosomes which might be due to its interaction with condensins or to indirect mechanisms provided by its interactions at the nuclear envelope.

Identification of a spindle-associated protein in ciliate micronuclei

1989 ◽  
Vol 93 (2) ◽  
pp. 287-298
Author(s):  
GUY KERYER ◽  
NICOLE GARREAU DE LOUBRESSE ◽  
NICOLE BORDES ◽  
MICHEL BORNENS
Keyword(s):  
Cell Cycle ◽  
Monoclonal Antibody ◽  
Nuclear Envelope ◽  
Mammalian Cells ◽  
Fibrous Material ◽  
Cortical Microtubule ◽  
Ciliated Protozoa ◽  
Paramecium Tetraurelia ◽  
Electron Microscope Level ◽  
Microtubule Organizing Centres

Ciliated protozoa display a nuclear dualism, with germinal micronuciei and a somatic macronucleus. During mitosis, which proceeds without disruption of the nuclear envelope, a spindle is organized within the micronucleus from, presumably, intranuclear microtubule-organizing centres (MTOCs). In order to characterize these MTOCs, monoclonal antibodies generated against human centrosomes were screened on several ciliates and particularly on Paramecium tetraurelia. In this ciliate, the monoclonal antibody CTR 532, which decorates centrosomal and spindle-associated components in mammalian cells, specifically labelled the micronuclei during interphase. At the electron-microscope level, it stained a fibrous material surrounding microtubules localized on the inner face of the nuclear envelope. During mitosis this decoration extended all over the metaphase spindle. At all stages of the cell cycle, the decoration remained specific to the micronucleus and was absent not only from all of the various cytoplasmic and cortical microtubule arrays but also from the macronuclei, even at early stages of their development from the zygotic nucleus. CTR 532 recognizes a single 170x103 Mr polypeptide in the cytoskeletal fraction that contains micronuclei and this polypeptide is absent in the cytoskeletal fraction of amicronucleate cells.

scholarly journals OASIS/CREB3L1 is a factor that responds to nuclear envelope stress

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Yasunao Kamikawa ◽  
Atsushi Saito ◽  
Koji Matsuhisa ◽  
Masayuki Kaneko ◽  
Rie Asada ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
Genome Instability ◽  
Nuclear Lamina ◽  
Nuclear Deformation ◽  
Membrane Domain ◽  
Stress Response Pathway ◽  
Envelope Stress ◽  
Genome Activity

AbstractThe nuclear envelope (NE) safeguards the genome and is pivotal for regulating genome activity as the structural scaffold of higher-order chromatin organization. NE had been thought as the stable during the interphase of cell cycle. However, recent studies have revealed that the NE can be damaged by various stresses such as mechanical stress and cellular senescence. These types of stresses are called NE stress. It has been proposed that NE stress is closely related to cellular dysfunctions such as genome instability and cell death. Here, we found that an endoplasmic reticulum (ER)-resident transmembrane transcription factor, OASIS, accumulates at damaged NE. Notably, the major components of nuclear lamina, Lamin proteins were depleted at the NE where OASIS accumulates. We previously demonstrated that OASIS is cleaved at the membrane domain in response to ER stress. In contrast, OASIS accumulates as the full-length form to damaged NE in response to NE stress. The accumulation to damaged NE is specific for OASIS among OASIS family members. Intriguingly, OASIS colocalizes with the components of linker of nucleoskeleton and cytoskeleton complexes, SUN2 and Nesprin-2 at the damaged NE. OASIS partially colocalizes with BAF, LEM domain proteins, and a component of ESCRT III, which are involved in the repair of ruptured NE. Furthermore, OASIS suppresses DNA damage induced by NE stress and restores nuclear deformation under NE stress conditions. Our findings reveal a novel NE stress response pathway mediated by OASIS.

scholarly journals Mutational analyses of fs(1)Ya, an essential, developmentally regulated, nuclear envelope protein in Drosophila.

Genetics ◽  
1995 ◽  
Vol 141 (4) ◽  
pp. 1473-1481 ◽  
Author(s):  
J Liu ◽  
K Song ◽  
M F Wolfner
Keyword(s):  
Cell Cycle ◽  
Embryonic Development ◽  
Nuclear Envelope ◽  
Envelope Protein ◽  
Chromatin Condensation ◽  
Cell Cycle Control ◽  
Nuclear Lamina ◽  
Mitotic Division ◽  
Developmentally Regulated ◽  
Egg Maturation

Abstract The fs(1)Ya protein (YA) is an essential, maternally encoded, nuclear lamina protein that is under both developmental and cell cycle control. A strong Ya mutation results in early arrest of embryos. To define the function of YA in the nuclear envelope during early embryonic development, we characterized the phenotypes of four Ya mutants alleles and determined their molecular lesions. Ya mutant embryos arrest with abnormal nuclear envelopes prior to the first mitotic division; a proportion of embryos from two leaky Ya mutants proceed beyond this but arrest after several abnormal divisions. Ya unfertilized eggs contain nuclei of different sizes and condensation states, apparently due to abnormal fusion of the meiotic products immediately after meiosis. Lamin is localized at the periphery of the uncondensed nuclei in these eggs. These results suggest that YA function is required during and after egg maturation to facilitate proper chromatin condensation, rather than to allow a lamin-containing nuclear envelope to form. Two leaky Ya alleles that partially complement have lesions at opposite ends of the YA protein, suggesting that the N- and C-termini are important for YA function and that YA might interact with itself either directly or indirectly.

scholarly journals Adenovirus E4orf4 protein induces PP2A-dependent growth arrest in Saccharomyces cerevisiae and interacts with the anaphase-promoting complex/cyclosome

2001 ◽  
Vol 154 (2) ◽  
pp. 331-344 ◽  
Author(s):  
Daniel Kornitzer ◽  
Rakefet Sharf ◽  
Tamar Kleinberger
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Cycle ◽  
Mammalian Cells ◽  
Growth Arrest ◽  
Anaphase Promoting Complex ◽  
Reading Frame ◽  
Cycle Growth ◽  
M Phase ◽  
Dependent Growth ◽  
Synthetically Lethal

Adenovirus early region 4 open reading frame 4 (E4orf4) protein has been reported to induce p53-independent, protein phosphatase 2A (PP2A)–dependent apoptosis in transformed mammalian cells. In this report, we show that E4orf4 induces an irreversible growth arrest in Saccharomyces cerevisiae at the G2/M phase of the cell cycle. Growth inhibition requires the presence of yeast PP2A-Cdc55, and is accompanied by accumulation of reactive oxygen species. E4orf4 expression is synthetically lethal with mutants defective in mitosis, including Cdc28/Cdk1 and anaphase-promoting complex/cyclosome (APC/C) mutants. Although APC/C activity is inhibited in the presence of E4orf4, Cdc28/Cdk1 is activated and partially counteracts the E4orf4-induced cell cycle arrest. The E4orf4–PP2A complex physically interacts with the APC/C, suggesting that E4orf4 functions by directly targeting PP2A to the APC/C, thereby leading to its inactivation. Finally, we show that E4orf4 can induce G2/M arrest in mammalian cells before apoptosis, indicating that E4orf4-induced events in yeast and mammalian cells are highly conserved.

scholarly journals Primase p49 mRNA expression is serum stimulated but does not vary with the cell cycle.

1989 ◽  
Vol 9 (5) ◽  
pp. 1940-1945 ◽  
Author(s):  
B Y Tseng ◽  
C E Prussak ◽  
M T Almazan
Keyword(s):  
Cell Cycle ◽  
Dna Synthesis ◽  
Mammalian Cells ◽  
Cell Cycle Progression ◽  
Small Subunit ◽  
Mrna Levels ◽  
Proliferating Cells ◽  
Restriction Point ◽  
Serum Stimulation ◽  
G1 Cells

Expression of the small-subunit p49 mRNA of primase, the enzyme that synthesizes oligoribonucleotides for initiation of DNA replication, was examined in mouse cells stimulated to proliferate by serum and in growing cells. The level of p49 mRNA increased approximately 10-fold after serum stimulation and preceded synthesis of DNA and histone H3 mRNA by several hours. Expression of p49 mRNA was not sensitive to inhibition by low concentrations of cycloheximide, which suggested that the increase in mRNA occurred before the restriction point control for cell cycle progression described for mammalian cells and was not under its control. p49 mRNA levels were not coupled to DNA synthesis, as observed for the replication-dependent histone genes, since hydroxyurea or aphidicolin had no effect on p49 mRNA levels when added before or during S phase. These inhibitors did have an effect, however, on the stability of p49 mRNA and increased the half-life from 3.5 h to about 20 h, which suggested an interdependence of p49 mRNA degradation and DNA synthesis. When growing cells were examined after separation by centrifugal elutriation, little difference was detected for p49 mRNA levels in different phases of the cell cycle. This was also observed when elutriated G1 cells were allowed to continue growth and then were blocked in M phase with colcemid. Only a small decrease in p49 mRNA occurred, whereas H3 mRNA rapidly decreased, when cells entered G2/M. These results indicate that the level of primase p49 mRNA is not cell cycle regulated but is present constitutively in proliferating cells.

scholarly journals Cell cycle-dependent effects on deoxyribonucleotide and DNA labeling by nucleoside precursors in mammalian cells.

1987 ◽  
Vol 7 (1) ◽  
pp. 532-534 ◽  
Author(s):  
J M Leeds ◽  
C K Mathews
Keyword(s):  
Cell Cycle ◽  
Mammalian Cells ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
G1 Phase ◽  
Ovary Cells ◽  
Dna Labeling ◽  
Metabolic Pool ◽  
Specific Activities ◽  
Cycle Dependent

dCTP pools equilibrated to equivalent specific activities in Chinese hamster ovary cells or in nuclei after incubation of cells with radiolabeled nucleosides, indicating that dCTP in nuclei does not constitute a distinct metabolic pool. In the G1 phase, [5-3H]deoxycytidine labeled dCTP to unexpectedly high specific activities. This may explain reports of replication-excluded DNA precursor pools.

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