By overexpression of gene constructs encoding nuclear lamin proteins in Xenopus oocytes we have shown that lamins B1 and B2, rather than being integrated into the endogenous lamina and forming thickened `fibrous laminae as repeatedly described in the literature [Fawcett and others (Fawcett, 1966; Höger et al., 1991), and references therein], induce the formation of intranuclear membrane-like structures that harbor the excess protein. By contrast, when genes encoding lamins A and LIII are overexpressed, the resulting proteins are targeted to the nuclear envelope and associate with the lamina in a manner indistinguishable from that of endogenous lamin LIII. These findings of differences between lamins are remarkable, as all four lamins are coexpressed in various combinations and relative ratios in different cell types during development and in adult tissues of Xenopus laevis.. Lamin LIII is the major constituent of the oocyte lamina (Stick and Krohne, 1982; Stick and Hausen, 1985; Stick, 1988), ...

Nuclear shape is different in stem cells and differentiated cells and reflects important changes in the mechanics of the nuclear envelope (NE). The current framework emphasizes the key role of the nuclear lamina in nuclear mechanics and its alterations in disease 1, 2 . Whether active stress controls nuclear deformations and how this stress interplays with properties of the NE to control NE dynamics is unclear. We address this in the early Drosophila embryo, where profound changes in NE shape parallel the transcriptional activation of the zygotic genome. We show that microtubule (MT) polymerization events produce the elementary forces necessary for NE dynamics. Moreover, large-scale NE-deformations associated with groove formation require concentration of microtubule polymerization in bundles organized by Dynein. However, MT bundles cannot produce grooves when the farnesylated inner nuclear membrane protein Charleston/Kugelkern (Char/Kuk) is absent 3, 4 . Although it increases stiffness of the NE, Char

The monoclonal antibody 414 is an excellent marker for NCSs. However, only a subset of the nucleoporins recognized by this antibody resides in NCSs: Nup153 and Nup62. Similarly, only some inner nuclear membrane (emerin) and lamina proteins (lamin A/C) are enriched in NCSs, whereas all tested proteins of the smooth endoplasmic reticulum are present. This selective composition of the NCS, together with its membrane tubules in the normally membrane-free nucleus, renders the NCS unique among nuclear organelles. Despite the analysis of only a sample of envelope proteins, it is clear that NCSs are not a mere extension but a specialization of the nuclear envelope.. Although membranous structures have been previously observed in nuclei, they were all artificially induced and differ in composition from the physiological NCSs as detailed below. R-rings, which are induced by exogenous expression of the nucleolar protein Nopp140, are virtually indistinguishable from NCSs at an ultrastructural level, hinting ...

Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.

We previously reported that the small nuclear RNA processing complex, Integrator, is required for dynein recruitment to the nuclear envelope at mitotic onset in cultured human cells. We now report an additional role for INT in ciliogenesis. Depletion of INT subunits from cultured human cells results in loss of primary cilia. We provide evidence that the requirements for INT in dynein localization and ciliogenesis are uncoupled: proteins essential for ciliogenesis are not essential for dynein recruitment to the nuclear envelope, while depletion of known regulators of perinuclear dynein has minimal effects on ciliogenesis. Taken together, our data support a model in which INT ensures proper processing of distinct pools of transcripts encoding components that independently promote perinuclear dynein enrichment and ciliogenesis.. ...

Mitosis is the process by which eukaryotic cells divide to form two equal daughter cells each with a copy of its genome. [86] Typically eukaryotic cells undergo one of the two forms of mitosis; higher eukaryotes (metazoans) go through Open Mitosis, while lower eukaryotes including yeast and other types of fungi undergo Closed Mitosis. [87] The distinction between open and closed mitosis can be made by focusing on the behaviour of the nuclear envelope which separates the nuclear contents from the cytoplasm and is split to form daughter nuclei. [86] Open mitosis is so named because the nuclear envelope completely breaks down at the transition from G2 to M stage of the cell cycle [87] and the nuclear content, including the genetic material, is open to mix with cytoplasmic macromolecules [88] until the nuclear envelope is reassembled after chromosomal segregation during telophase/G1. [87] [88] In contrast, during closed mitosis the nuclear envelope remains intact and mitosis continues within the ...

Deciphering novel pathways that regulate liver lipid content has profound implications for understanding the pathophysiology of nonalcoholic fatty liver disease (NAFLD) and nonalcoholic steatohepatitis (NASH). Recent evidence suggests that the nuclear envelope is a site of regulation of lipid metabolism, but there is limited appreciation of the responsible mechanisms and molecular components within this organelle. We showed that conditional hepatocyte deletion of the inner nuclear membrane protein lamina-associated polypeptide 1 (LAP1) causes defective VLDL secretion and steatosis, including intranuclear lipid accumulation. LAP1 binds to and activates torsinA, an AAA+ ATPase that resides in the perinuclear space and continuous main ER. Deletion of torsinA from mouse hepatocytes caused even greater reductions in VLDL secretion and profound steatosis. Mice from both of the mutant lines studied developed hepatic steatosis and subsequent steatohepatitis on a regular chow diet in the absence of ...

The barrier-to-autointegration factor BAF binds to the LEM domain (Em(LEM)) of the nuclear envelope protein emerin and plays an essential role in the nuclear architecture of metazoan cells. In addition, the BAF(2) dimer bridges and compacts double-stranded DNA nonspecifically via two symmetry-relate …

DNA calls for the return of the nuclear envelope (NE) after mitosis, according to Ulbert et al. (page 469). The abundance of DNA may thus be one reason why the NE reforms so quickly.. NE reformation occurs so quickly that breaking down the process in vivo has so far been impossible. Many scientists instead use in vitro reconstitution assays, which indicate that chromatin decondensation (as occurs at the end of mitosis) initiates the recruitment of vesicle populations to chromatin. In the new work, the authors aimed to identify membrane and chromatin components that mediate this recruitment and thus NE assembly.. The main component of chromatin is, of course, DNA. The group found that excess naked DNA prevented in vitro NE reformation by titrating vesicles away from chromatin at early stages. DNA alone was a more potent inhibitor than chromatin, although chromatin proteins might also contribute, particularly later on as the envelope matures.. DNA does not bind pure liposomes, so the authors next ...

Spermiogenesis describes the differentiation of haploid germ cells into motile, fertilization-competent spermatozoa. During this fundamental transition the species-specific sperm head is formed, which necessitates profound nuclear restructuring coincident with the assembly of sperm-specific structures and chromatin compaction. In the case of the mouse, it is characterized by reshaping of the early round spermatid nucleus into an elongated sickle-shaped sperm head. This tremendous shape change requires the transduction of cytoskeletal forces onto the nuclear envelope (NE) or even further into the nuclear interior. LINC (linkers of nucleoskeleton and cytoskeleton) complexes might be involved in this process, due to their general function in bridging the NE and thereby physically connecting the nucleus to the peripheral cytoskeleton. LINC complexes consist of inner nuclear membrane integral SUN-domain proteins and outer nuclear membrane KASH-domain counterparts. SUN- and KASH-domain proteins are ...

Spermiogenesis describes the differentiation of haploid germ cells into motile, fertilization-competent spermatozoa. During this fundamental transition the species-specific sperm head is formed, which necessitates profound nuclear restructuring coincident with the assembly of sperm-specific structures and chromatin compaction. In the case of the mouse, it is characterized by reshaping of the early round spermatid nucleus into an elongated sickle-shaped sperm head. This tremendous shape change requires the transduction of cytoskeletal forces onto the nuclear envelope (NE) or even further into the nuclear interior. LINC (linkers of nucleoskeleton and cytoskeleton) complexes might be involved in this process, due to their general function in bridging the NE and thereby physically connecting the nucleus to the peripheral cytoskeleton. LINC complexes consist of inner nuclear membrane integral SUN-domain proteins and outer nuclear membrane KASH-domain counterparts. SUN- and KASH-domain proteins are ...

The nuclear membrane serves as a barrier between the nucleus and the cytoplasm, allowing controlled gene regulation and transcription in the nuclear area (CALLAN HG et al, 1950; WATSON ML. 1955). The nuclear pores allow for active transport of small molecules, but also larger proteins, between the nucleus and the cytoplasm (Paine PL et al, 1975; BAHR GF et al, 1954). In that sense, the nuclear membrane creates both a barrier, but also a linkage between the nucleus and the rest of the cell. The nuclear membrane is a highly dynamic structure and the structural composition is altered throughout the cell cycle. During the G2 phase, the nuclear membrane expands as a result of chromosome duplication. The membrane breaks down in the prometaphase to enable connection of the centrosomes and the spindle apparatus to the sister chromatids during mitosis. The breakdown mechanism involves disassembly of the nuclear pore complexes, depolymerization of the nuclear lamina, removal of proteins associated ...

Laminopathies are a group of rare genetic disorders caused by mutations in genes encoding proteins of the nuclear lamina. They are included in the more generic term nuclear envelopathies that was coined in 2000 for diseases associated with defects of the nuclear envelope.[2] Since the first reports of laminopathies in the late 1990s, increased research efforts have started to uncover the vital role of nuclear envelope proteins in cell and tissue integrity in animals.

Gram-negative bacteria possess a unique and complex cell envelope, composed of an inner and outer membrane separated by an intermediate cell wall-containing periplasm. This tripartite structure acts intrinsically as a significant biological barrier, often limiting the permeation of anti-infectives, and so preventing such drugs from reaching their target. Furthermore, identification of the specific permeation-limiting envelope component proves difficult in the case of many anti-infectives, due to the challenges associated with isolation of individual cell envelope structures in bacterial culture. The development of an in vitro permeation model of the Gram-negative inner membrane, prepared by repeated coating of physiologically-relevant phospholipids on Transwell®filter inserts, is therefore reported, as a first step in the development of an overall cell envelope model. Characterization and permeability investigations of model compounds as well as anti-infectives confirmed the suitability of the ...

Annulate lamella is one of cell membrane classes, occurring as set of parallel elemernts with duble same dimensional membranes, as the nuclear envelope. These lamella have pore complexes which are identical to those of the nuclear cover. It is arranged in highly ordered structure with a regular specing between themselves. These lamella are characteristic for the oocytes, spermatocytes, some somatic and cancer cels. They are characteristic of actively growing cells, including many functions in genetic information transfer and storage. They are probably formed from the nuclear envelope. Similar membranes are found in both the cytoplasm and nucleoplasm. In the nucleoplasm, they are small, irrrgular, as well as short-living. It have been established that, in some condition, ribosomes being directly connected to the annulate lamellar membrane, supposing a role in the process of protein synthesis. Cell membranes Nuclear envelope Rieger R. Michaelis A.; Green M. M. (1976). Glossary of genetics and ...

The nuclear envelope (NE) surrounds the nucleus and separates it from the cytoplasm. The NE is not a passive structural component, but rather contributes to various cellular processes such as genome organization, transcription, signaling, and stress responses. Although the NE is mostly a smooth

View pdf The replication of herpesviruses, including human cytomegalovirus (HCMV), is based on a nuclear phase followed by viral egress through the nuclear envelope. For nuclear egress, the transient destabilization of the nuclear envelope, notably the nuclear lamina, is an event with central importance. The destabilization of this rigid proteinaceous network is achieved by the function of lamina-associated effector proteins (HCMV egress proteins) which particularly recruit protein kinases to phosphorylate nuclear lamins. This process is reminiscent of a similar sequence of events occurring during cellular mitosis. In contrast to mitosis, however, nuclear destabilization during HCMV replication does not involve the entire nuclear envelope but is restricted to locally defined areas and this reprogramming seems to be achieved by a small number of viral effectors. Thus, the virus-specific nuclear destabilization is based on the formation and activity of a viral-cellular nuclear egress complex ...

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Conventional organization of a mammalian nucleus. Different landmarks contribute to genome segregation into functional compartments. The nuclear envelope defines the edge of the nucleus. The nuclear lamina is a meshwork of proteins that interact with heterochromatic genomic regions called lamina-associated domains (LADs), only interrupted by nuclear pore complexes (NPC). The two main other landmarks: the chromocenter, composed of clustered pericentromeric heterochromatin (PCH), and the nucleolus. (right) region of the nucleus with the histone marks associated with the different compartments. LADs at the periphery are enriched in H3K9me2/3 modifications and H3K27me3 at LAD borders. Heterochromatin regions show different levels of HP1 with higher concentration at PCH. The NPC interacts with euchromatin domains. Ac, acetylation; me2/3, di or tri-methylation; DNA 5mC, DNA methylation; HP1, Heterochromatin Protein 1; LBR, Lamin B Receptor; NET, Nuclear Envelope Transmembrane protein. After Canat , ...

Nuclei move to specific locations to polarize migrating and differentiating cells. material during cell division (1-3). Most nuclear motions are microtubule-mediated; however growing numbers of actin-dependent nuclear motions have been acknowledged (1 2 4 Mechanisms for actin-dependent nuclear movement are unclear. In NIH3T3 fibroblasts polarizing for migration into in vitro wounds an actin-dependent nuclear movement is definitely induced by serum or the serum element lysophosphatidic acid (LPA) and this reorients the centrosome toward the leading edge (5). Nuclear movement and actin retrograde circulation happen at the same rate but how actin is definitely coupled to the nucleus is definitely unfamiliar. We explored the possible involvement of the LINC (linker of nucleoskeleton and cytoskeleton) complex which spans the inner and outer nuclear membranes (INM and ONM respectively). LINC complexes consist of ONM nesprin and INM SUN proteins and have been implicated in microtubule-dependent but not ...

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Functional analysis of centrosomal kinase substrates in Drosophila melanogaster reveals a new function of the nuclear envelope component otefin in cell cycle progression Habermann K, Mirgorodskaya E, Gobom J, Lehmann V, Müller H, Blümlein K, Deery MJ, Czogiel I, Erdmann C, Ralser M, von Kries JP, Lange BM Mol Cell Biol. 2012 32(17):3554-69 ...

Habermann, K.; Mirgorodskaya, E.; Gobom, J.; Lehmann, V.; Müller, H.; Blümlein, K.; Deery, M. J.; Czogiel, I.; Erdmann, C.; Ralser, M. et al.; von Kries, J. P.; Lange, B. M. H.: Functional analysis of centrosomal kinase substrates in Drosophila melanogaster reveals a new function of the nuclear envelope component otefin in cell cycle progression. Molecular and Cellular Biology (Washington, DC) 32 (17), S. 3554 - 3569 (2012 ...

Beginning on page 809, Adams and Kilmartin describe an extensive series of experiments that reveal some of the key components of S. cerevisiae spindle pole body (SPB) duplication. The SPB, functionally equivalent to the centrosome of higher eukaryotes, is duplicated on the intact nuclear envelope during yeast mitosis. A structure next to the SPB, called the half-bridge, appears to direct the assembly of a spherical satellite, which is later replaced by the new SPB, but the molecular details of this process were poorly understood.. After studying SPB duplication by EM and determining that a plaque-like structure replaces the satellite at intermediate stages of duplication, Adams and Kilmartin identified the SPB core components by mass spectrometry. Immunoelectron microscopy with GFP-tagged versions of these proteins showed that some SPB components are common to the satellite and the plaque-like structure, suggesting that the new structure is built around the satellite. Finally, ...

Authors: Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie. Citation: Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie. 1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin Biomol. NMR Assign. 10, 179-182 (2016).. Assembly members: ...

It is made up of two layers, each made up of a lipid bilayer. lipid bilayer is enveloped with holes, called nuclear pores, to regulate the exchange of substances (for example, proteins and RNA) between the nucleus and the cytoplasm. Perinuclear space is space between membranes. The outer membrane is contiguous with the endoplasmic reticulum. The inner membrane is constituted by a network of filaments called nuclear lamina, The lamina attach to chromosomes. It also acts like a shield for the nucleus. ...

Interaction between actin filaments (AFs) and microtubules (MTs) has been reported in various plant cells, and the presence of a factor(s) connecting these two cytoskeletal networks has been suggested, but its molecular entity has not been elucidated yet. We obtained a fraction containing MT-binding polypeptides, which induced bundling of AFs and of MTs. A 190 kDa polypeptide which associated with AFs was selectively isolated from the fraction. This polypeptide was thought to have an ability to bind to both AFs and MTs. We raised a monoclonal antibody against the 190 kDa polypeptide. Immunostaining demonstrated the association of the 190 kDa polypeptide with AF bundles and with MT bundles formed in vitro. Immunocytochemical studies throughout the cell cycle revealed that the 190 kDa polypeptide was localized in the nucleus before nuclear envelope breakdown, and in the spindle and the phragmoplast during cell division. After the re-formation of the nuclear envelope, the 190 kDa polypeptide was ...

To find out, the researchers examined postmortem tissue from AD and control brains. They noticed that unlike the smooth, rounded neuronal nuclei of controls, those in AD brains appeared wrinkled and folded (see image at left). Some nucleoporins with disordered domains had seeped out into the cytoplasm instead of staying in the pores.. The group decided to focus on Nup98, a particularly abundant and highly disordered nucleoporin. High-resolution optical microscopy revealed that p-tau co-localized with Nup98 at the nuclear surface in hippocampal neurons from AD patients. In p-tau containing nuclei, Nup98 left the nuclear membrane and co-localized with more than 90 percent of tau tangles sitting in the cytoplasm. Other Nups stayed put in the nuclear membrane, suggesting the bulk of the complex remained, just in an altered form.. Did the two proteins interact directly? In surface plasmon resonance experiments, p-tau bound the N-terminus of Nup98. The C-terminus of this nucleoporin contains many ...

Nesprin-1 and nesprin-2 (also known as Syne-1 and Syne-2,) are large ( approximately 3300-residue) vertebrate proteins associated with emerin and lamin A at the nuclear envelope of muscle cells and other cell types. We show that the previously described nesprins are short isoforms of giant proteins …

Die Universität zu Köln ist eine Exzellenzuniversität mit dem klassischen Fächerspektrum einer Volluniversität. Als eine der größen Hochschulen Europas arbeitet sie in Forschung und Lehre auch international auf höchstem Niveau.

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The nuclear membrane dissolves during the prometaphase of mitosis, while it disintegrates during prometaphase I and prometaphase II of meiosis. The breakdown of the nuclear envelope is due to the...

The spatial arrangement of chromatin within the nucleus can affect reactions that occur on the DNA and is likely to be regulated. Here we show that activation of INO1 occurs at the nuclear membrane and requires the integral membrane protein Scs2. Scs2 antagonizes the action of the transcriptional repressor Opi1 under conditions that induce the unfolded protein response (UPR) and, in turn, activate INO1. Whereas repressed INO1 localizes throughout the nucleoplasm, the gene is recruited to the nuclear periphery upon transcriptional activation. Recruitment requires the transcriptional activator Hac1, which is produced upon induction of the UPR, and is constitutive in a strain lacking Opi1. Artificial recruitment of INO1 to the nuclear membrane permits activation in the absence of Scs2, indicating that the intranuclear localization of a gene can profoundly influence its mechanism of activation. Gene recruitment to the nuclear periphery, therefore, is a dynamic process and appears to play an ...

At the nuclear envelope, the nuclear lamina and heterochromatin are adjacent to the inner nuclear membrane. CBX3 binds DNA and is a component of…

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Concept 13: Meiosis II: Telophase II. A nuclear envelope forms around each set of chromosomes and cytokinesis occurs, producing four daughter cells, each with a haploid set of chromosomes. To see telophase II. A nuclear envelope forms around each set of chromosomes. ...

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In memory donation envelopes are available on request. These can be made available at a funeral, wake, church or other commemorative services where people may choose to make a donation to MS Research Australia. The donation envelopes can then be collected and sent to us, or your guests can mail them to us directly.. To request donation envelopes please contact the MS Research Australia office on 1300 356 467 or email.. ...

The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis.

Eukaryotic cells are defined by the presence of a nucleus containing the DNA genome and bound by a nuclear membrane (or nuclear envelope) composed of two lipid bilayers that regulate transport of materials into and out of the nucleus through nuclear pores. Eukaryotic cell morphologies vary greatly and may be maintained by various structures, including the cytoskeleton, the cell membrane, and/or the cell wall The nucleolus in the nucleus of eukaryotic cells is the site of ribosomal synthesis ...

Baudrimont A, Penkner A, Woglar A, Machacek T, Wegrostek C, Gloggnitzer J, Fridkin A, Klein F, Gruenbaum Y, Pasierbek P, Jantsch V. (2010). Leptotene/zygotene chromosome movement via the SUN/KASH protein bridge in Caenorhabditis elegans. PLoS Genet. 6(11):e1001219. (abstract). Baumann CL, Aspalter IM, Sharif O, Pichlmair A, Blüml S, Grebien F, Bruckner M, Pasierbek P, Aumayr K, Planyavsky M, Bennett KL, Colinge J, Knapp S, Superti-Furga G. (2010). CD14 is a coreceptor of Toll-like receptors 7 and 9.J Exp Med. 207(12):2689-701. (abstract). Hoelbl, A., Schuster, C., Kovacic, B., Zhu, B., Wickre, M., Hoelzl, MA., Fajmann, S., Grebien, F., Warsch, W., Stengl, G., Hennighausen, L., Poli, V., Beug, H., Moriggl, R., Sexl, V. (2010). Stat5 is indispensable for the maintenance of bcr/abl-positive leukaemia. EMBO Mol Med. 2(3):98-110 (abstract) Pospisilik, JA., Schramek, D., Schnidar, H., Cronin, SJ., Nehme, NT., Zhang, X., Knauf, C., Cani, PD., Aumayr, K., Todoric, J., Bayer, M., Haschemi, A., ...

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Alvarez-Fernández M, Sánchez-Martínez R, Sanz-Castillo B, Gan PP, Sanz-Flores M, Trakala M, Ruiz-Torres M, Lorca T, Castro A, Malumbres M (2013). Greatwall is essential to prevent mitotic collapse after nuclear envelope breakdown in mammals. Proc Natl Acad Sci USA 110, 17374-17379 ...

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The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins, a family of 50 to 100 proteins, are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene belongs to the nucleoporin family and is associated with the oncogenic nucleoporin CAN/Nup214 in a dynamic subcomplex. This protein is also overexpressed in a large number of malignant neoplasms and precancerous dysplasias. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Mar 2016 ...

The single spanning INM protein emerin is encoded by the EMD gene, which, when mutated, produces the X‐linked form of Emery-Dreifuss muscular dystrophy (EDMD; Gruenbaum et al, 2005). The lamin‐associated protein LAP2β was originally identified as a single spanning INM protein with a nucleoplasmic binding region for lamin B and chromatin (Foisner & Gerace, 1993). Both emerin and LAP2β associate with several transcriptional regulators, and this association invariably coincides with repression of the transcription factor target genes. In most instances, the mechanism of repression is not clear because it is uncertain whether the transcription factor acts as an activator or repressor of transcription-often transcription factors can do both. If the transcription factor acts as an activator, sequestering the transcription factor away from its target gene is a possible mechanism. If the transcription factor acts as a repressor, a model would be created of a repressive environment for the target ...

Lamins are type V intermediate filaments and represent the major constituent of the nuclear lamina. Mutations in the laminA/C gene as well as in other nuclear envelope associated proteins lead to a series of human genetic disorders, so-called laminopathies. The most prominent laminopathy is the Hutchinson-Gilford progeria syndrome (HGPS). HGPS patients appear prematurely aged developing aging-related conditions such as osteoporosis, loss of subcutaneous fat and cardiovaskular disease already during childhood. Many of the HGPS patients contain a single point mutation in the lamin A/C gene wh ...

TY - JOUR. T1 - Nuclear pore protein NUP88 activates anaphasepromoting complex to promote aneuploidy. AU - Naylor, Ryan M.. AU - Jeganathan, Karthik B.. AU - Cao, Xiuqi. AU - Van Deursen, Jan. PY - 2016/2/1. Y1 - 2016/2/1. N2 - The nuclear pore complex protein NUP88 is frequently elevated in aggressive human cancers and correlates with reduced patient survival; however, it is unclear whether and how NUP88 overexpression drives tumorigenesis. Here, we show that mice overexpressing NUP88 are cancer prone and form intestinal tumors. To determine whether overexpression of NUP88 drives tumorigenesis, we engineered transgenic mice with doxycycline-inducible expression of Nup88. Surprisingly, NUP88 overexpression did not alter global nuclear transport, but was a potent inducer of aneuploidy and chromosomal instability. We determined that NUP88 and the nuclear transport factors NUP98 and RAE1 comprise a regulatory network that inhibits premitotic activity of the anaphase-promoting complex/cyclosome ...

The nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm. Nuclear pores in turn allow the transport of water-soluble molecules across the nuclear envelope. Nucleoporins, a family of around 30 proteins, are the main components of the nuclear pore complex in eukaryotic cells. Nucleoporin 62 is the most abundant member of this family. Nucleoporins are able to transport molecules across the nuclear envelope at a very high rate. A single NPC is able to transport 60,000 protein molecules across the nuclear envelope every minute. Nucleoporins mediate transport of macromolecules between the cell nucleus and cytoplasm in eukaryotes. Certain members of the nucleoporin family form the structural scaffolding of the nuclear pore complex. However, ...

In this work, the geometrical characteristics of two different types of cells observed with Electron Microscopy were analysed. The nuclear envelope of Wild-type HeLa cells and Chlamydia trachomatis-infected HeLa cells were automatically segmented and then modelled against a spheroid and converted to a two-dimensional surface. Geometric measurements from this surface and the volumetric nuclear envelope were extracted to compare the two types of cells. The measurements included the nuclear volume, the sphericity of the nucleus, its flatness or spikiness. In total 13 different cells were segmented: 7 Wild-type and 6 Chlamydia trachomatis-infected. The cells were statistically different in the following measurements. Wild-type HeLa cells have greater volumes than that of Chlamydia trachomatis-infected HeLa cells and they are more spherical as Jaccard index suggests. Standard deviation (σ), and range of values for the nuclear envelope, which shows the distance of the highest peaks and deepest ...

Meckel-Gruber syndrome (MKS) is a severe autosomal recessively inherited disorder caused by mutations in genes that encode components of the primary cilium and basal body. Here we show that two MKS proteins, MKS1 and meckelin, that are required for centrosome migration and ciliogenesis interact with actin-binding isoforms of nesprin-2 (nuclear envelope spectrin repeat protein 2, also known as Syne-2 and NUANCE). Nesprins are important scaffold proteins for maintenance of the actin cytoskeleton, nuclear positioning and nuclear-envelope architecture. However, in ciliated-cell models, meckelin and nesprin-2 isoforms colocalized at filopodia prior to the establishment of cell polarity and ciliogenesis. Loss of nesprin-2 and nesprin-1 shows that both mediate centrosome migration and are then essential for ciliogenesis, but do not otherwise affect apical-basal polarity. Loss of meckelin (by siRNA and in a patient cell-line) caused a dramatic remodelling of the actin cytoskeleton, aberrant localization ...

Detection of autoantibodies giving nuclear rim pattern by immunofluorescence (anti-nuclear envelope antibodies - ANEA) in sera from patients with primary biliary cirrhosis (PBC) is a useful tool for the diagnosis and prognosis of the disease. Differences in the prevalence of ANEA in PBC sera so far reported have been attributed to the methodology used for the detection as well as to ethnic/geographical variations. Therefore, we evaluated the prevalence of ANEA in sera of Greek patients with PBC by using methods widely used by clinical laboratories and a combination of techniques and materials. We screened 103 sera by immunoblotting on nuclear envelopes and indirect immunofluorescence (IIF) using cells and purified nuclei. Reactivities against specific autoantigens were assessed using purified proteins, ELISA, immunoprecipitation and mass spectrometry. We found higher prevalence of ANEA when sera were assayed by IIF on purified nuclei or cultured cells (50%) compared to Hep2 commercially available slides

Nuclear pore complexes. Coloured atomic force micrograph (AFM) of the surface of an oocyte (egg cell) nucleus showing the nuclear pore complexes (NPCs). NPCs are complexes of proteins that are embedded in the nuclear envelope. All material moving between the nucleus and the cell cytoplasm passes through these channels. They allow passive transport (diffusion) of ions and small molecules and active transport (energy dependent) of proteins and RNAs (ribonucleic acids). - Stock Image G455/0064

We have identified a component of the human nuclear pore complex and have shown that it is the product of a gene involved in oncogenic activation. A monoclonal antibody raised against purified nuclear matrix proteins recognizes a single protein with an electrophoretic mobility of approximately 300 kDa and stains the nuclear envelope in a punctate pattern typical of nuclear pores. The antibody was used to screen lambda gt11 human cDNA libraries, and the resulting clones were sequenced and compared to sequences in the Genbank database. An exact match was found with the human tpr (for translocated promoter region) gene, a gene shown previously to be involved in the oncogenic activation of several protein kinases. Double-label immunofluorescent microscopy with the anti-Tpr antibody and an antibody to the previously characterized nuclear pore complex protein nup153 confirms that Tpr is localized to the nuclear pore complex. Tpr is located on the cytoplasmic face of the nucleus, as demonstrated by

Nagase T et al. (1996) Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain.. ...

Nuclear pore complexes are fixed in place [http://jcb.rupress.org/cgi/content/abstract/154/1/71 Daigle et al.] report that nuclear pore complexes (NPCs) undergo [http://jcb.rupress.org/cgi/content/full/200101089/F4/DC1 limited movements] that match the deformations of the nuclear envelope as tracked using a [http://jcb.rupress.org/cgi/content/full/200101089/F4/DC2 grid] of bleached nuclear lamins. NPCs are therefore remarkably stable complexes, and are probably anchored to a protein network in the nuclear envelope ...

During its lifetime, a nucleus may be broken down or destroyed, either in the process of cell division or as a consequence of apoptosis (the process of programmed cell death). During these events, the structural components of the nucleus - the envelope and lamina - can be systematically degraded. In most cells, the disassembly of the nuclear envelope marks the end of the prophase of mitosis. However, this disassembly of the nucleus is not a universal feature of mitosis and does not occur in all cells. Some unicellular eukaryotes (e.g., yeasts) undergo so-called closed mitosis, in which the nuclear envelope remains intact. In closed mitosis, the daughter chromosomes migrate to opposite poles of the nucleus, which then divides in two. The cells of higher eukaryotes, however, usually undergo open mitosis, which is characterized by breakdown of the nuclear envelope. The daughter chromosomes then migrate to opposite poles of the mitotic spindle, and new nuclei reassemble around them. At a certain ...

Author Summary Development of multicellular organisms such as humans requires appropriate activation of gene expression programs according to stages of differentiation. Many proteins that directly regulate this process have been identified, including histone-modifying enzymes and transcription factors. It is not clear whether nuclear pore proteins, proteins that form the only channels in the nuclear envelope that mediate nuclear transport, regulate developmental gene regulation in higher organisms such as humans. Here we show that one nuclear pore protein has a role in gene regulation during human cell differentiation, providing insight into the development-related and transport-independent function of nuclear pore proteins. We have found that the nuclear pore protein interacts with the human genome in a dynamic manner that is tightly linked to the developmental stage. In addition, manipulating the functional levels of the nuclear pore protein can disrupt expression of the developmental genes it

LMNA-related disorders are caused by mutations in the LMNA gene, which encodes for the nuclear envelope proteins, lamin A and C, via alternative splicing. Laminopathies are associated with a wide range of disease phenotypes, including neuromuscular, cardiac, metabolic disorders and premature aging syndromes. The most frequent diseases associated with mutations in the LMNA gene are characterized by skeletal and cardiac muscle involvement. This review will focus on genetics and clinical features of laminopathies affecting primarily skeletal muscle. Although only symptomatic treatment is available for these patients, many achievements have been made in clarifying the pathogenesis and improving the management of these diseases.

Maturation of the mammalian oocyte is characterized in part by dissolution of the nuclear envelope, or germinal vesicle breakdown (GVB). By fluorescence microscopy after vital uptake of acridine orange (AO), redistribution and perinuclear accumulation of organelles corresponding to lysosomes occur before GVB in rat oocytes undergoing meiotic maturation in vitro. In follicle-enclosed oocytes explanted during the preovulatory gonadotropin surge (GS) and individually cultured as such in chemically defined medium at approximately 22 degrees C, lysosomes aggregated into disperse clusters after 30 min; by 60 min, perinuclear concentration of lysosomes and their essential disappearance from the cortical ooplasm were observed. GVB occurred within 120 min. In contrast, follicle-enclosed oocytes explanted before the GS displayed a generally homogeneous distribution of lysosomes and intact GV for up to 5 h in culture. In oocytes aspirated from follicles before the GS, partially denuded of granulosa cells, ...

Nuclear pore complexes (NPCs) are ∼100 MDa transport channels assembled from multiple copies of ∼30 nucleoporins (Nups). One-third of these Nups contain phenylalanine-glycine (FG)-rich repeats, forming a diffusion barrier, which is selectively permeable for nuclear transport receptors that interact with these repeats. Here, we identify an additional function of FG repeats in the structure and biogenesis of the yeast NPC. We demonstrate that GLFG-containing FG repeats directly bind to multiple scaffold Nups in vitro and act as NPC-targeting determinants in vivo. Furthermore, we show that the GLFG repeats of Nup116 function in a redundant manner with Nup188, a nonessential scaffold Nup, to stabilize critical interactions within the NPC scaffold needed for late steps of NPC assembly. Our results reveal a previously unanticipated structural role for natively unfolded GLFG repeats as Velcro to link NPC subcomplexes and thus add a new layer of connections to current models of the NPC architecture. ...

Read the Abcam customer review (11128) for Anti-Lamin B1 antibody - Nuclear Envelope Marker used in Western blot. Abcam provides excellent in-house scientific support

(Phys.org)-Two teams of researchers taking different approaches have successfully mapped and diagramed the nuclear pore complex (NPC)-protein complexes that make up the pores in the nuclear envelope that allow or prevent ...

Plant cells can exhibit highly complex nuclear organization. Through dye-labeling experiments in untransformed onion epidermal and tobacco culture cells and through the expression of green fluorescent protein targeted to either the nucleus or the lumen of the endoplasmic reticulum/nuclear envelope in these cells, we have visualized deep grooves and invaginations into the large nuclei of these cells. In onion, these structures, which are similar to invaginations seen in some animal cells, form tubular or planelike infoldings of the nuclear envelope. Both grooves and invaginations are stable structures, and both have cytoplasmic cores containing actin bundles that can support cytoplasmic streaming. In dividing tobacco cells, invaginations seem to form during cell division, possibly from strands of the endoplasmic reticulum trapped in the reforming nucleus. The substantial increase in nuclear surface area resulting from these grooves and invaginations, their apparent preference for association with ...

Abcam provides specific protocols for Anti-Nuclear Pore Complex Proteins antibody [39C7] (ab60080) : Flow cytometry protocols, Immunocytochemistry &…

The enclosure of nuclear contents in eukaryotes means that cells require sites in the boundary that mediate exchange of material between nucleus and cytoplasm. These sites, termed nuclear pore complexes (NPCs), number 100-200 in yeast, a few thousand in mammalian cells and approximately 50 million in the giant nuclei of amphibian oocytes. NPCs are large (125 MDa) macromolecular complexes that comprise 50-100 different proteins in vertebrates. In spite of their size and complex structure, NPCs undergo complete breakdown and reformation at cell division. Transport through NPCs can be rapid (estimated at several hundred molecules/pore/second) and accommodates both passive diffusion of relatively small molecules, and active transport of complexes up to several megadaltons in molecular mass. Each pore can facilitate both import and export. The two processes apparently involve multiple pathways for different cargoes, and their transport signals, transport receptors and adapters, and the molecules (and ...

Nucleoporin 50 (Nup50) is a protein that in humans is encoded by the NUP50 gene.[1][2] The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. The protein encoded by this gene is a member of the FG-repeat containing nucleoporins that functions as a soluble cofactor in importin-alpha:beta-mediated nuclear protein import. Pseudogenes of this gene are found on chromosomes 5, 6, and 14. Two transcript variants encoding different isoforms have been found for this gene.[2] ...

Emerin and LEM2 are ubiquitous inner nuclear membrane protein conserved from human beings to pets that were possibly hypomorphic (LEM-2-null and heterozygous for Ce-emerin) or null for both protein. LEM-2-null pets 4-Epi Minocycline showed unexpected flaws in smooth muscles activity. These results implicate individual LEM2 mutations being a potential reason behind EDMD and further suggest […]. ...

FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] The nuclear envelope creates distinct nuclear and cytoplasmic compartments in eukaryotic cells. It consists of two concentric membranes perforated by nuclear pores, large protein complexes that form aqueous channels to regulate the flow of macromolecules between the nucleus and the cytoplasm. These complexes are composed of at least 100 different polypeptide subunits, many of which belong to the nucleoporin family. The nucleoporin protein encoded by this gene displays evolutionarily conserved interactions with other nucleoporins. This protein, which localizes to both sides of the nuclear pore complex at interphase, remains associated with the complex during mitosis and is targeted at early stages to the reforming nuclear envelope. This protein also localizes to kinetochores of mitotic cells. [provided by RefSeq, Jul 2008 ...

Nuclear pores are the primary gatekeepers mediating communication between a cells nucleus and its cytoplasm. Recently these large multiprotein transport channels have also been shown to play an essential role in developmental gene regulation. Despite the critical role in nuclear function, however, nuclear pore complexes remain somewhat shadowy figures, with many details about their formation shrouded in mystery.. Now a team of investigators from the Salk Institute for Biological Studies has illuminated key differences in the mechanisms behind nuclear pores formed at two distinct stages in the cell cycle. Their findings, to be published in the June 12 issue of Cell, may provide insights into conditions such as cancer, developmental defects, and sudden cardiac arrest.. Nuclear pores, which are built from 30 different proteins, assemble during interphase, the period when the nucleus expands and replicates its DNA, and following mitosis, when the nuclear membrane reforms around the segregated ...

This chapter focuses on the role of bacterial cell surfaces in catalyzing biomineralization processes and in promoting microfossil formation. Ultrathin sections were prepared by conventional embedding without the addition of osmium tetroxide or uranyl acetate as heavy-metal fixatives and contrasting agents. The electron density in these ultrathin sectioned samples as well as in the whole mounts presented in this chapter was provided by the naturally immobilized metals. The domains Bacteria and the Archaea represent the two major bacterial groups that have been identified based on 16S rRNA phylogenetic studies. The domain Bacteria is divided into the gram-positive or gram-negative groups based on cell envelope structure and chemistry (although gram-variable organisms also exist). The formation of many secondary minerals in natural as well as laboratory systems is catalyzed by microorganisms. These precipitation reactions have been divided into two general categories: passive and active mineralization.

HIV vaccines were not part of the main stage at the Durban Aids Conference held in 2000. Our knowledge and experience in HIV vaccine development were rudimentary at this time; our journey to understanding the complexity of designing immunogens to elicit effective immune responses was just beginning. But HIV vaccines are a now pivotal part of the prevention research agenda: there is scientific optimism about the ability to develop an effective vaccine and South Africa is now a central point in this research. The intervening 16 years between the Durban conferences has brought a series of hard-won understandings about how HIV works in orchestrating its transmission from person to person and between communities. Our past approaches to vaccine development have largely been ineffective because the viruss exterior coating, what we call its envelope structure, has areas of immune dampening. In these areas, immune decoys are set up and evolve so cleverly that the initial, critical antibodies that are made to

Nuclear membrane pore. Illustration of the structure of a pore in the membrane (envelope) of a cell nucleus. These pores contain proteins that control and facilitate the movement of molecules into and out of the nucleus, especially ones related to nucleic acids such as DNA and RNA. The nuclear envelope (blue) is a double membrane. The nuclear pore (orange) consists of a central channel (cylindrical), a nuclear basket (bottom), cytoplasmic filaments (top), and a ring of proteins (centre). For this artwork without labels, see image C023/8734. - Stock Image C023/8733

ID: http://www.ncbi.nlm.nih.gov/gene/57122 Type: http://bio2vec.net/ontology/gene Label: NUP107 Synonyms: NUP107, NPHS11, NUP84, nucleoporin 107, nuclear pore complex protein Nup107, nucleoporin 107kDa Alternative IDs: 57122 API: GO SPARQL: GO ...

N Panté, U Aebi; The nuclear pore complex. J Cell Biol 1 September 1993; 122 (5): 977-984. doi: https://doi.org/10.1083/jcb.122.5.977. Download citation file:. ...

Bidirectional transport of macromolecules between the cytoplasm and nucleus occurs through nuclear pore complexes (NPCs) embedded in the nuclear envelope. NPCs are composed of subcomplexes, and NUP43 is part of one such subcomplex, Nup107-160 (Loiodice et al., 2004 [PubMed 15146057]).[supplied by OMIM, Mar 2008 ...

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David R. McIlwain, Philipp A. Lang, Thorsten Maretzky, Koichi Hamada, Kazuhito Ohishi, Sathish Kumar Maney, Thorsten Berger, Aditya Murthy, Duncan, G., Xu, H.C., Lang, K.S., Häussinger, D., Wakeham, A., Youten, A.I., Khokha, R., Ohashi, P.S., Blobel, C.P. and Mak, T.W. 2012. iRhom2 regulates innate immunity via TACE/ADAM17. Science 335(6065):229-32. Glomski, K., Monette, S., Manova, K., De Strooper, B., Saftig, P., and Blobel, C.P. 2011. Deletion of ADAM10 in endothelial cells leads to defects in organ-specific vascular structures. Blood 118(4):1163-74. Maretzky, T., Evers, A., Zhou, W., Swendeman, S.L., Wong, P.-M., Rafii, S., Reiss, K., and Blobel, C.P. 2011. Migration of growth factor-stimulated epithelial and endothelial cells depends on EGFR transactivation by ADAM17. Nature Comm. 2:229. Brandl, K., Sun, L., Neppl, C., Siggs, O.M., Le Gall, S.M., Tomisato, W., Li, X., Du, X., Maennel, D.N., Blobel, C.P., Beutler, B. 2010. MyD88 signaling in nonhematopoietic cells protects mice against ...

Export GlyConnect protein list related to glycosylation_site_structure with id 287800011800008849 P49790 # id : 2878 Nuclear pore complex protein Nup153 Homo sapiens ...

Nuclear pore complexes (NPCs) are the gates that allow passage of molecules and macromolecules across the nuclear envelope. NPCs are composed of about 30 nucleoporins (Nups) that form a conserved supramolecular assembly with eight‐fold symmetry of ∼60 MDa in yeast and ∼120 MDa in vertebrates (Hetzer et al, 2005; Tran and Wente, 2006). Electron microscopy studies revealed the overall architecture of the NPC, which consists of a central spoke-ring assembly to which the cytoplasmic filaments and the nuclear basket are attached (Akey and Radermacher, 1993; Yang et al, 1998; Allen et al, 2000; Fahrenkrog and Aebi, 2003). A central transport channel is formed by the spoke-ring complex, which is filled up by a meshwork of natively unfolded Phe‐Gly (FG) repeats that are part of a class of nucleoporins (Patel et al, 2007). Current models emphasize how the FG repeats are organized within the central transport channel to generate the permeability barrier for passive diffusion of molecules through ...

Gene Information Bidirectional transport of macromolecules between the cytoplasm and nucleus occurs through nuclear pore complexes (NPCs) embedded in the nuclear envelope. NPCs are composed of subcomplexes and NUP37 is part of one such subcomplex Nup107-160 (Loiodice et al. 2004 [PubMed 15146057]).[supplied by OMIM Mar 2008]. ...

Our lab is interested in several aspects of the cytoskeleton, ranging from biochemical and cell biological aspects to genetic aspects. Proteins of interest are cyclase-associated protein (CAP), coronin, the Nesprins which together with the SUN proteins form the LINC complex (Linker of nucleoskeleton and cytoskeleton), and centrosomal proteins which are associated with human disease states.. Keywords: Actin cytoskeleton & dynamics / Dictyostelium & mouse models / functional & comparative genome analysis / nuclear envelope / centrosome & disease. Subject area(s): Cell & Tissue Architecture , Genomic & Computational Biology , Molecular Medicine. ...

ASTMC136319Red-Standard Test Method for Thermal Performance of Building Materials and Envelope Assemblies by Means of a Hot Box Apparatus (Standard + Redline

FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] Nucleoporins are proteins that play an important role in the assembly and functioning of the nuclear pore complex (NPC) which regulates the movement of macromolecules across the nuclear envelope (NE). The protein encoded by this gene plays a role in the fusion of NE vesicles and formation of the double membrane NE. The protein may also be involved in cardiac physiology and may be associated with the pathogenesis of atrial fibrillation. Alternative splicing results in multiple transcript variants of this gene. A pseudogene associated with this gene is located on chromosome 6. [provided by RefSeq, May 2013 ...

TY - JOUR. T1 - Influence of the nuclear membrane, active transport, and cell shape on the Hes1 and p53-Mdm2 pathways. T2 - Bulletin of Mathematical Biology. AU - Sturrock,Marc. AU - Terry,Alan J.. AU - Xirodimas,Dimitris P.. AU - Thompson,Alastair M.. AU - Chaplain,Mark A. J.. PY - 2012/7. Y1 - 2012/7. N2 - There are many intracellular signalling pathways where the spatial distribution of the molecular species cannot be neglected. These pathways often contain negative feedback loops and can exhibit oscillatory dynamics in space and time. Two such pathways are those involving Hes1 and p53-Mdm2, both of which are implicated in cancer.In this paper we further develop the partial differential equation (PDE) models of Sturrock et al. (J. Theor. Biol., 273:15-31, 2011) which were used to study these dynamics. We extend these PDE models by including a nuclear membrane and active transport, assuming that proteins are convected in the cytoplasm towards the nucleus in order to model transport along ...

The spindle pole body (SPB) of yeast organizes microtubules and is essential for chromosome segregation. The SPB duplicates once per cell cycle and subsequently becomes inserted into the nuclear envelope (NE). In this study, Rüthnick et al. describe how a nuclear pore complex becomes recruited to the new SPB during the duplication process. Disturbance of this recruitment process prevents insertion of the new SPB into the NE. ...