scholarly journals Cell-specific modulation of nuclear pore complexes controls cell cycle entry during asymmetric division

2017 ◽  
Author(s):  
Arun Kumar ◽  
Priyanka Sharma ◽  
Zhanna Shcheprova ◽  
Anne Daulny ◽  
Trinidad Sanmartín ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Fate ◽  
Daughter Cell ◽  
Asymmetric Division ◽  
Nuclear Accumulation ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Cell Cycle Entry ◽  
Independent Functions ◽  
Pore Complexes

SummaryThe acquisition of cellular identity is coupled to changes in the nuclear periphery and nuclear pore complexes (NPCs). Whether and how these changes determine cell fate remains unclear. We have uncovered a mechanism regulating NPC acetylation to direct cell fate after asymmetric division in budding yeast. The lysine deacetylase Hos3 associates specifically with daughter cell NPCs during mitosis to delay cell cycle entry (Start). Hos3-dependent deacetylation of nuclear basket and central channel nucleoporins establishes daughter cell-specific nuclear accumulation of the transcriptional repressor Whi5 during anaphase and perinuclear silencing of the CLN2 gene in the following G1 phase. Hos3-dependent coordination of both events restrains Start in daughter but not in mother cells. We propose that deacetylation modulates transport-dependent and - independent functions of NPCs, leading to differential cell cycle progression in mother and daughter cells. Similar mechanisms might regulate NPC functions in specific cell types and/or cell cycle stages in multicellular organisms.

scholarly journals Daughter-cell-specific modulation of nuclear pore complexes controls cell cycle entry during asymmetric division

2018 ◽  
Vol 20 (4) ◽  
pp. 432-442 ◽  
Author(s):  
Arun Kumar ◽  
Priyanka Sharma ◽  
Mercè Gomar-Alba ◽  
Zhanna Shcheprova ◽  
Anne Daulny ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Daughter Cell ◽  
Asymmetric Division ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Cell Cycle Entry ◽  
Pore Complexes

scholarly journals Ensuring that yeast cells get their inheritance

2013 ◽  
Vol 203 (2) ◽  
pp. 167-167
Author(s):  
Mitch Leslie
Keyword(s):  
Daughter Cell ◽  
Yeast Cells ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Pore Complexes

A nucleoporin allows nuclear pore complexes access to daughter cell during mitosis.

scholarly journals Spatial control of nucleoporin assembly by Fragile X-related proteins

2019 ◽  
Author(s):  
Arantxa Agote-Arán ◽  
Stephane Schmucker ◽  
Katerina Jerabkova ◽  
Inès Jmel Boyer ◽  
Alessandro Berto ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Nuclear Envelope ◽  
Fragile X Syndrome ◽  
Cell Cycle Progression ◽  
Fragile X ◽  
Nuclear Pore ◽  
Nuclear Morphology ◽  
Nuclear Pore Complexes ◽  
Cycle Progression ◽  
Pore Complexes

SummaryNucleoporins (Nups) build highly organized Nuclear Pore Complexes (NPCs) at the nuclear envelope (NE). Several Nups assemble into a sieve-like hydrogel within the central channel of the NPCs to regulate nucleocytoplasmic exchange. In the cytoplasm, a large excess of soluble Nups has been reported, but how their assembly is restricted to the NE is currently unknown. Here we show that Fragile X-related protein 1 (FXR1) can interact with several Nups and facilitate their localization to the NE during interphase through a microtubule and dynein-dependent mechanism. Downregulation of FXR1 or closely related orthologs FXR2 and Fragile X mental retardation protein (FMRP) leads to the accumulation of cytoplasmic Nup protein condensates. Likewise, several models of Fragile X syndrome (FXS), characterized by a loss of FMRP, also accumulate cytoplasmic Nup aggregates. These aggregate-containing cells display aberrant nuclear morphology and a delay in G1 cell cycle progression. Our results reveal an unexpected role for the FXR protein family and dynein in the spatial regulation of nucleoporin assembly.HighlightsCytoplasmic nucleoporins are assembled by Fragile X-related (FXR) proteins and dyneinFXR-Dynein pathway downregulation induces aberrant cytoplasmic aggregation of nucleoporinsCellular models of Fragile X syndrome accumulate aberrant cytoplasmic nucleoporin aggregates.FXR-Dynein pathway regulates nuclear morphology and G1 cell cycle progressioneTOC BlurbNucleoporins (Nups) form Nuclear Pore Complexes (NPCs) at the nuclear envelope. Agote-Arán at al. show how cells inhibit aberrant assembly of Nups in the cytoplasm and identify Fragile X-related (FXR) proteins and dynein that facilitate localization of Nups to the nuclear envelope and control G1 cell cycle progression.Graphical abstract

scholarly journals Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes.

1995 ◽  
Vol 6 (4) ◽  
pp. 401-417 ◽  
Author(s):  
O Li ◽  
C V Heath ◽  
D C Amberg ◽  
T C Dockendorff ◽  
C S Copeland ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Messenger Rna ◽  
Nuclear Periphery ◽  
Nuclear Accumulation ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Permissive Temperature ◽  
Temperature Dependent ◽  
Pore Complexes ◽  
Mutant Cells

To identify genes whose products play potential roles in the nucleocytoplasmic export of messenger RNA, we isolated temperature-sensitive strains of Saccharomyces cerevisiae and examined them by fluorescent in situ hybridization. With the use of a digoxigen-tagged oligo-(dT)50 probe, we identified those that showed nuclear accumulation of poly(A)+ RNA when cells were shifted to the nonpermissive temperature. We describe here the properties of yeast strains bearing the rat3-1 mutation (RAT-ribonucleic acid trafficking) and the cloning of the RAT3 gene. When cultured at the permissive temperature of 23 degrees C, fewer than 10% of cells carrying the rat3-1 allele showed nuclear accumulation of poly(A)+ RNA, whereas approximately 70% showed nuclear accumulation of poly(A)+ RNA, whereas approximately 70% showed nuclear accumulation of poly(A)+ RNA after a shift to 37 degrees C for 4 h. In wild-type cells, nuclear pore complexes (NPCs) are distributed relatively evenly around the nuclear envelope. Both indirect immunofluorescence analysis and electron microscopy of rat3-1 cells indicated that NPCs were clustered into one or a few regions of the NE in mutant cells. Similar NPC clustering was seen in mutant cells cultured at temperatures between 15 degrees C and 37 degrees C. The RAT3 gene encodes an 1157-amino acid protein without similarity to other known proteins. It is essential for growth only at 37 degrees C. Cells carrying a disruption of the RAT3 gene were very similar to cells carrying the original rat3-1 mutation; they showed temperature-dependent nuclear accumulation of poly(A)+ RNA and exhibited constitutive clustering of NPCs. Epitope tagging of Rat3p demonstrated that it is located at the nuclear periphery and co-localizes with nuclear pore proteins recognized by the RL1 monoclonal antibody. We refer to this nucleoporin as Rat3p/Nup133p.

scholarly journals Synchronization of Interphase Events Depends neither on Mitosis nor on cdk1

2003 ◽  
Vol 14 (9) ◽  
pp. 3730-3740 ◽  
Author(s):  
Ayelet Laronne ◽  
Shay Rotkopf ◽  
Asaf Hellman ◽  
Yosef Gruenbaum ◽  
Andrew C.G. Porter ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Dna Replication ◽  
Ubiquitin Ligase ◽  
Nuclear Membrane ◽  
Nuclear Lamina ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Polyploid Cells ◽  
Dividing Cells ◽  
Pore Complexes

Human HT2-19 cells with a conditional cdk1 mutation stop dividing upon cdk1 inactivation and undergo multiple rounds of endoreplication. We show herein that major cell cycle events remain synchronized in these endoreplicating cells. DNA replication alternates with gap phases and cell cycle-specific cyclin E expression is maintained. Centrosomes duplicate in synchrony with chromosome replication, giving rise to polyploid cells with multiple centrosomes. Centrosome migration, a typical prophase event, also takes place in endoreplicating cells. The timing of these events is unaffected by cdk1 inactivation compared with normally dividing cells. Nuclear lamina breakdown, in contrast, previously shown to be dependent on cdk1, does not take place in endoreplicating HT2-19 cells. Moreover, breakdown of all other major components of the nuclear lamina, like the inner nuclear membrane proteins and nuclear pore complexes, seems also to depend on cdk1. Interestingly, the APC/C ubiquitin ligase is activated in these endoreplicating cells by fzr but not by fzy. The oscillations of interphase events are thus independent of cdk1 and of mitosis but may depend on APC/Cfzr activity.

scholarly journals Autophagy of the Nucleus in Health and Disease

2022 ◽  
Vol 9 ◽  
Author(s):  
Georgios Konstantinidis ◽  
Nektarios Tavernarakis
Keyword(s):  
Cell Cycle ◽  
Dna Damage ◽  
Cellular Differentiation ◽  
Nuclear Material ◽  
Nuclear Pore ◽  
Common Denominator ◽  
Nuclear Pore Complexes ◽  
The Core ◽  
Health And Disease ◽  
Pore Complexes

Nucleophagy is an organelle-selective subtype of autophagy that targets nuclear material for degradation. The macroautophagic delivery of micronuclei to the vacuole, together with the nucleus-vacuole junction-dependent microautophagic degradation of nuclear material, were first observed in yeast. Nuclear pore complexes and ribosomal DNA are typically excluded during conventional macronucleophagy and micronucleophagy, indicating that degradation of nuclear cargo is tightly regulated. In mammals, similarly to other autophagy subtypes, nucleophagy is crucial for cellular differentiation and development, in addition to enabling cells to respond to various nuclear insults and cell cycle perturbations. A common denominator of all nucleophagic processes characterized in diverse organisms is the dependence on the core autophagic machinery. Here, we survey recent studies investigating the autophagic processing of nuclear components. We discuss nucleophagic events in the context of pathology, such as neurodegeneration, cancer, DNA damage, and ageing.

scholarly journals Essential Roles for Caenorhabditis elegans Lamin Gene in Nuclear Organization, Cell Cycle Progression, and Spatial Organization of Nuclear Pore Complexes

2000 ◽  
Vol 11 (11) ◽  
pp. 3937-3947 ◽  
Author(s):  
Jun Liu ◽  
Tom Rolef Ben-Shahar ◽  
Dieter Riemer ◽  
Millet Treinin ◽  
Perah Spann ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Caenorhabditis Elegans ◽  
Cell Cycle Progression ◽  
Spatial Organization ◽  
Nuclear Periphery ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Cycle Progression ◽  
Nuclear Lamins ◽  
Pore Complexes

Caenorhabditis elegans has a single lamin gene, designated lmn-1 (previously termed CeLam-1). Antibodies raised against the lmn-1 product (Ce-lamin) detected a 64-kDa nuclear envelope protein. Ce-lamin was detected in the nuclear periphery of all cells except sperm and was found in the nuclear interior in embryonic cells and in a fraction of adult cells. Reductions in the amount of Ce-lamin protein produce embryonic lethality. Although the majority of affected embryos survive to produce several hundred nuclei, defects can be detected as early as the first nuclear divisions. Abnormalities include rapid changes in nuclear morphology during interphase, loss of chromosomes, unequal separation of chromosomes into daughter nuclei, abnormal condensation of chromatin, an increase in DNA content, and abnormal distribution of nuclear pore complexes (NPCs). Under conditions of incomplete RNA interference, a fraction of embryos escaped embryonic arrest and continue to develop through larval life. These animals exhibit additional phenotypes including sterility and defective segregation of chromosomes in germ cells. Our observations show thatlmn-1 is an essential gene in C. elegans, and that the nuclear lamins are involved in chromatin organization, cell cycle progression, chromosome segregation, and correct spacing of NPCs.

scholarly journals RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly

2004 ◽  
Vol 164 (7) ◽  
pp. 965-971 ◽  
Author(s):  
Sowmya Swaminathan ◽  
Florian Kiendl ◽  
Roman Körner ◽  
Raffaella Lupetti ◽  
Ludger Hengst ◽  
...  
Keyword(s):  
Cyclin B1 ◽  
Nucleocytoplasmic Transport ◽  
Nuclear Accumulation ◽  
Stable Complex ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
M Phase ◽  
Pore Complexes

The RanGTPase activating protein RanGAP1 has essential functions in both nucleocytoplasmic transport and mitosis. In interphase, a significant fraction of vertebrate SUMO1-modified RanGAP1 forms a stable complex with the nucleoporin RanBP2/Nup358 at nuclear pore complexes. RanBP2 not only acts in the RanGTPase cycle but also is a SUMO1 E3 ligase. Here, we show that RanGAP1 is phosphorylated on residues T409, S428, and S442. Phosphorylation occurs before nuclear envelope breakdown and is maintained throughout mitosis. Nocodazole arrest leads to quantitative phosphorylation. The M-phase kinase cyclin B/Cdk1 phosphorylates RanGAP1 efficiently in vitro, and T409 phosphorylation correlates with nuclear accumulation of cyclin B1 in vivo. We find that phosphorylated RanGAP1 remains associated with RanBP2/Nup358 and the SUMO E2–conjugating enzyme Ubc9 in mitosis, hence mitotic phosphorylation may have functional consequences for the RanGTPase cycle and/or for RanBP2-dependent sumoylation.

High resolution analysis of mammalian nuclear structure throughout the cell cycle: implications for nuclear pore complex assembly during interphase and mitosisThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell.

2006 ◽  
Vol 84 (3-4) ◽  
pp. 423-430 ◽  
Author(s):  
Sheona P. Drummond ◽  
Sandra A. Rutherford ◽  
Helen S. Sanderson ◽  
Terry D. Allen
Keyword(s):  
Cell Cycle ◽  
Mammalian Cells ◽  
Molecular Transport ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
High Resolution Analysis ◽  
Multiple Copies ◽  
A Cell ◽  
Specific Proteins ◽  
Pore Complexes

Nuclear pore complexes (NPCs) are the gateways for both active and passive bidirectional molecular transport between the nucleoplasm and cytoplasm. These mega-dalton assemblies are composed of multiple copies of approximately 30 distinct proteins termed nucleoporins. Higher eukaryotes display an “open” mitosis in which the NPCs, nuclear envelope, and lamina disassemble. During mitosis several nucleoporins are redistributed to kinetochores until they are recruited back to the periphery of chromatin as the NPCs are reassembled. Within this study we have developed and optimized the visualization of mammalian cells and their chromosome profiles throughout the cell-cycle. Close attention has been paid to the preservation of chromatin, membranes, and NPC structure to investigate the ultrastructural locations of specific proteins in both interphase and mitosis.

scholarly journals cut11 +: A Gene Required for Cell Cycle-dependent Spindle Pole Body Anchoring in the Nuclear Envelope and Bipolar Spindle Formation in Schizosaccharomyces pombe

1998 ◽  
Vol 9 (10) ◽  
pp. 2839-2855 ◽  
Author(s):  
Robert R. West ◽  
Elena V. Vaisberg ◽  
Rubai Ding ◽  
Paul Nurse ◽  
J. Richard McIntosh
Keyword(s):  
Cell Cycle ◽  
Nuclear Envelope ◽  
Fluorescent Protein ◽  
Spindle Pole ◽  
Early Prophase ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Spindle Formation ◽  
Bipolar Spindle ◽  
Pore Complexes

The “cut” mutants of Schizosaccharomyces pombeare defective in spindle formation and/or chromosome segregation, but they proceed through the cell cycle, resulting in lethality. Analysis of temperature-sensitive alleles of cut11 +suggests that this gene is required for the formation of a functional bipolar spindle. Defective spindle structure was revealed with fluorescent probes for tubulin and DNA. Three-dimensional reconstruction of mutant spindles by serial sectioning and electron microscopy showed that the spindle pole bodies (SPBs) either failed to complete normal duplication or were free floating in the nucleoplasm. Localization of Cut11p tagged with the green fluorescent protein showed punctate nuclear envelope staining throughout the cell cycle and SPBs staining from early prophase to mid anaphase. This SPB localization correlates with the time in the cell cycle when SPBs are inserted into the nuclear envelope. Immunoelectron microscopy confirmed the localization of Cut11p to mitotic SPBs and nuclear pore complexes. Cloning and sequencing showed thatcut11 + encodes a novel protein with seven putative membrane-spanning domains and homology to theSaccharomyces cerevisiae gene NDC1. These data suggest that Cut11p associates with nuclear pore complexes and mitotic SPBs as an anchor in the nuclear envelope; this role is essential for mitosis.

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