scholarly journals The nuclear-envelope protein and transcriptional repressor LAP2  interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation

2005 ◽  
Vol 118 (17) ◽  
pp. 4017-4025 ◽  
Author(s):  
R. Somech
Keyword(s):  
Nuclear Envelope ◽  
Envelope Protein ◽  
Nuclear Periphery ◽  
Transcriptional Repressor ◽  
Histone H4 ◽  
Histone H4 Deacetylation

scholarly journals Genomic loci mispositioning in Tmem120a knockout mice yields latent lipodystrophy

2021 ◽  
Author(s):  
Rafal Czapiewski ◽  
Dzmitry G Batrakou ◽  
Jose I de las Heras ◽  
Roderick N Carter ◽  
Aishwarya Sivakumar ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nuclear Envelope ◽  
Envelope Protein ◽  
Nuclear Periphery ◽  
Genome Organisation ◽  
Partial Lipodystrophy ◽  
Lipodystrophy Syndrome ◽  
Metabolic Defects ◽  
Pathway Gene ◽  
Obesogenic Diet

Little is known about the proteins that direct the highly conserved patterns of spatial genome organisation in fat. Here we report that adipocyte-specific knockout of the gene encoding nuclear envelope protein Tmem120a disrupts fat genome organisation, thus causing a novel lipodystrophy syndrome. Tmem120a deficiency broadly suppresses lipid metabolism pathway gene expression and induces myogenic gene expression by repositioning genes, enhancers and miRNA-encoding loci between the nuclear periphery and interior. Tmem120a-/- mice, particularly females, exhibit a lipodystrophy syndrome similar to human familial partial lipodystrophy FPLD2, with profound insulin resistance and metabolic defects that manifests upon exposure to an obesogenic diet. Interestingly, similar genome organisation defects occurred in cells from FPLD2 patients that harbour nuclear envelope protein laminA mutations. Our data suggest TMEM120A may mediate/instigate novel categories of adipose tissue dysfunction across the adiposity spectrum and provide a new miRNA-based mechanism possibly driving the unexplained muscle hypertrophy in human lipodystrophy.

scholarly journals A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance

2007 ◽  
Vol 178 (5) ◽  
pp. 813-827 ◽  
Author(s):  
Alaron Lewis ◽  
Rachael Felberbaum ◽  
Mark Hochstrasser
Keyword(s):  
Nuclear Envelope ◽  
Nuclear Pore Complex ◽  
Envelope Protein ◽  
Mrna Export ◽  
Nuclear Periphery ◽  
Nuclear Pore ◽  
Nucleocytoplasmic Trafficking ◽  
Sumo Protease ◽  
Mrna Surveillance ◽  
Regulatory Event

The nuclear pore complex (NPC) is both the major conduit for nucleocytoplasmic trafficking and a platform for organizing macromolecules at the nuclear envelope. We report that yeast Esc1, a non-NPC nuclear envelope protein, is required both for proper assembly of the nuclear basket, a structure extending into the nucleus from the NPC, and for normal NPC localization of the Ulp1 SUMO protease. In esc1Δ cells, Ulp1 and nuclear basket components Nup60 and Mlp1 no longer distribute broadly around the nuclear periphery, but co-localize in a small number of dense-staining perinuclear foci. Loss of Esc1 (or Nup60) alters SUMO conjugate accumulation and enhances ulp1 mutant defects. Similar to previous findings with Mlp1, both Esc1 and Ulp1 help retain unspliced pre-mRNAs in the nucleus. Therefore, these proteins are essential for proper nuclear basket function, which includes mRNA surveillance and regulation of SUMO protein dynamics. The results raise the possibility that NPC-localized protein desumoylation may be a key regulatory event preventing inappropriate pre-mRNA export.

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 The Tor Pathway Regulates Gene Expression by Linking Nutrient Sensing to Histone Acetylation

2003 ◽  
Vol 23 (2) ◽  
pp. 629-635 ◽  
Author(s):  
John R. Rohde ◽  
Maria E. Cardenas
Keyword(s):  
Gene Expression ◽  
Cell Growth ◽  
Histone Acetylation ◽  
Nutrient Sensing ◽  
Gene Promoters ◽  
Histone H4 ◽  
Tor Pathway ◽  
Histone H4 Acetylation ◽  
Promoter Occupancy ◽  
Histone H4 Deacetylation

ABSTRACT The Tor pathway mediates cell growth in response to nutrient availability, in part by inducing ribosomal protein (RP) gene expression via an unknown mechanism. Expression of RP genes coincides with recruitment of the Esa1 histone acetylase to RP gene promoters. We show that inhibition of Tor with rapamycin releases Esa1 from RP gene promoters and leads to histone H4 deacetylation without affecting promoter occupancy by Rap1 and Abf1. Genetic and biochemical evidence identifies Rpd3 as the major histone deacetylase responsible for reversing histone H4 acetylation at RP gene promoters in response to Tor inhibition by rapamycin or nutrient limitation. Our results illustrate that the Tor pathway links nutrient sensing with histone acetylation to control RP gene expression and cell growth.

Sequential degradation of proteins from the nuclear envelope during apoptosis

2001 ◽  
Vol 114 (20) ◽  
pp. 3643-3653 ◽  
Author(s):  
Madeleine Kihlmark ◽  
Gabriela Imreh ◽  
Einar Hallberg
Keyword(s):  
Nuclear Envelope ◽  
Apoptotic Cell ◽  
Nuclear Periphery ◽  
Condensed Chromatin ◽  
Nuclear Pore ◽  
Dependent Manner ◽  
Nuclear Pores ◽  
Double Labeling ◽  
Lamin B ◽  
Nuclear Apoptosis

We have produced new antibodies specific for the integral pore membrane protein POM121. Using these antibodies we show that during apoptosis POM121 becomes proteolytically degraded in a caspase-dependent manner. The POM121 antibodies and antibodies specific for other proteins of the nuclear envelope were used in a comparative study of nuclear apoptosis in staurosporine-treated buffalo rat liver cells. Nuclei from these cells were classified in three different stages of apoptotic progression: stage I, moderately condensed chromatin surrounded by a smooth nuclear periphery; stage II, compact patches of condensed chromatin collapsing against a smooth nuclear periphery; stage III, round compact chromatin bodies surrounded by grape-shaped nuclear periphery. We have performed double labeling immunofluorescence microscopy of individual apoptotic cells and quantitative immunoblotting analysis of total proteins from apoptotic cell cultures. The results showed that degradation of nuclear envelope marker proteins occurred in a specific order. POM121 degradation occurred surprisingly early and was initiated before nucleosomal DNA degradation could be detected using TUNEL assay and completed before clustering of the nuclear pores. POM121 was eliminated significantly more rapid compared with NUP153 (a peripheral protein located in the nucleoplasmic basket of the nuclear pore complex) and lamin B (a component of the nuclear lamina). Disappearance of NUP153 and lamin B was coincident with onset of DNA fragmentation and clustering of nuclear pores. By contrast, the peripheral NPC protein p62 was degraded much later. The results suggest that degradation of POM121 may be an important early step in propagation of nuclear apoptosis.

The Nuclear Envelope Protein Emerin and Its Interacting Proteins

2016 ◽  
pp. 1-9
Author(s):  
Carol M Collins ◽  
Kimbre A Nee ◽  
James M Holaska
Keyword(s):  
Nuclear Envelope ◽  
Envelope Protein ◽  
Interacting Proteins

scholarly journals Architecture of the Nuclear Periphery of Rat Pachytene Spermatocytes: Distribution of Nuclear Envelope Proteins in Relation to Synaptonemal Complex Attachment Sites

1999 ◽  
Vol 10 (4) ◽  
pp. 1235-1245 ◽  
Author(s):  
Manfred Alsheimer ◽  
Elisabeth von Glasenapp ◽  
Robert Hock ◽  
Ricardo Benavente
Keyword(s):  
Nuclear Envelope ◽  
Synaptonemal Complex ◽  
Meiotic Prophase ◽  
Nuclear Periphery ◽  
Cell Fractionation ◽  
Nuclear Interior ◽  
Meiotic Chromosomes ◽  
Attachment Sites ◽  
Form Part ◽  
Pachytene Spermatocytes

The nucleus of spermatocytes provides during the first meiotic prophase an interesting model for investigating relationships of the nuclear envelope (NE) with components of the nuclear interior. During the pachytene stage, meiotic chromosomes are synapsed via synaptonemal complexes (SCs) and attached through both ends to the nuclear periphery. This association is dynamic because chromosomes move during the process of synapsis and desynapsis that takes place during meiotic prophase. The NE of spermatocytes possesses some peculiarities (e.g., lower stability than in somatic cells, expression of short meiosis-specific lamin isoforms called C2 and B3) that could be critically involved in this process. For better understanding of the association of chromosomes with the nuclear periphery, in the present study we have investigated the distribution of NE proteins in relation to SC attachment sites. A major outcome was the finding that lamin C2 is distributed in the form of discontinuous domains at the NE of spermatocytes and that SC attachment sites are embedded in these domains. Lamin C2 appears to form part of larger structures as suggested by cell fractionation experiments. According to these results, we propose that the C2-containing domains represent local reinforcements of the NE that are involved in the proper attachment of SCs.

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