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Nuclear pore complex

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https://www.readbyqxmd.com/read/28515232/the-nuclear-export-factor-crm1-controls-juxta-nuclear-microtubule-dependent-virus-transport
#1
I-Hsuan Wang, Christoph J Burckhardt, Artur Yakimovich, Matthias K Morf, Urs F Greber
Transport of large cargo through the cytoplasm requires motor proteins and polarized filaments. Viruses that replicate in the nucleus of post-mitotic cells use microtubules and the dynein/dynactin motor to traffic to the nuclear membrane, and deliver their genome through nuclear pore complexes (NPCs) into the nucleus. How virus particles (virions) or cellular cargo are transferred from microtubules to the NPC is unknown. Here, we analyzed trafficking of incoming cytoplasmic adenoviruses by single particle tracking and super-resolution microscopy...
May 17, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28506894/the-functional-versatility-of-the-nuclear-pore-complex-proteins
#2
REVIEW
Mohammed Hezwani, Birthe Fahrenkrog
Over the past few decades, it is increasingly evident that nucleoporins are multi-functional proteins that are not only pivotal for the formation of the nuclear pore complex. They also have key roles in mitosis, gene expression, development and disease. In this review, the versatility and functions of nucleoporins outside the NPC will be discussed.
May 12, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28506892/the-roles-of-the-nuclear-pore-complex-in-cellular-dysfunction-aging-and-disease
#3
REVIEW
Stephen Sakuma, Maximiliano A D'Angelo
The study of the Nuclear Pore Complex (NPC), the proteins that compose it (nucleoporins), and the nucleocytoplasmic transport that it controls has revealed an unexpected layer to pathogenic disease onset and progression. Recent advances in the study of the regulation of NPC composition and function suggest that the precise control of this structure is necessary to prevent diseases from arising or progressing. Here we discuss the role of nucleoporins in a diverse set of diseases, many of which directly or indirectly increase in occurrence and severity as we age, and often shorten the human lifespan...
May 12, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28506891/viral-mechanisms-for-docking-and-delivering-at-nuclear-pore-complexes
#4
REVIEW
Justin W Flatt, Urs F Greber
Some viruses possess the remarkable ability to transport their genomes across nuclear pore complexes (NPCs) for replication inside the host cell's intact nuclear compartment. Viral mechanisms for crossing the restrictive NPC passageway are highly complex and astonishingly diverse, requiring in each case stepwise interaction between incoming virus particles and components of the nuclear transport machinery. Exactly how a large viral genome loaded with accessory proteins is able to pass through the relatively narrow central channel of the NPC without causing catastrophic structural damage is not yet fully understood...
May 12, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28506890/biomechanics-of-the-transport-barrier-in-the-nuclear-pore-complex
#5
REVIEW
George J Stanley, Ariberto Fassati, Bart W Hoogenboom
The nuclear pore complex (NPC) is the selective gateway through which all molecules must pass when entering or exiting the nucleus. It is a cog in the gene expression pathway, an entrance to the nucleus exploited by viruses, and a highly-tuned nanoscale filter. The NPC is a large proteinaceous assembly with a central lumen occluded by natively disordered proteins, known as FG-nucleoporins (or FG-nups). These FG-nups, along with a family of soluble proteins known as nuclear transport receptors (NTRs), form the selective transport barrier...
May 12, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28490590/the-c-terminus-of-the-herpes-simplex-virus-pul25-protein-is-required-for-release-of-viral-genomes-from-capsids-bound-to-nuclear-pores
#6
Jamie B Huffman, Gina R Daniel, Erik Falck-Pedersen, Alexis Huet, Greg A Smith, James F Conway, Fred L Homa
The herpes simplex virus (HSV) capsid is released into the cytoplasm after fusion of viral and host membranes, whereupon dynein-dependent trafficking along microtubules targets it to the nuclear envelope. Binding of the capsid to the nuclear pore complex (NPC) is mediated by the capsid protein pUL25 and the capsid-tethered tegument protein pUL36. Temperature-sensitive mutants in both pUL25 and pUL36 dock at the NPC but fail to release DNA. The uncoating reaction has been difficult to study due to the rapid release of the genome once the capsid interacts with the nuclear pore...
May 10, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28476938/chromatin-organization-at-the-nuclear-periphery-as-revealed-by-image-analysis-of-structured-illumination-microscopy-data
#7
Jindřiška Fišerová, Michaela Efenberková, Tomáš Sieger, Miloslava Maninová, Jana Uhlířová, Pavel Hozák
Nuclear periphery (NP) plays substantial role in chromatin organization. Heterochromatin at the NP is intermitted with active chromatin surrounding nuclear pore complexes (NPCs), however, details of the peripheral chromatin organization are missing. To discern the distributions of epigenetic marks at the NP of HeLa nuclei, we used structured illumination microscopy combined with a new MATLAB software tool for an automatic NP and NPC detection, measurements of fluorescent intensity and statistical analysis of measured data...
May 5, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28473267/functional-implication-of-the-common-evolutionary-origin-of-nuclear-pore-complex-and-endomembrane-management-systems
#8
REVIEW
Ivan Liashkovich, Victor Shahin
Nuclear pore complexes (NPCs) are the sole gateway between the cytoplasm and the nucleus serving both as stringent permeability barrier and active transporters between the two compartments of eukaryotic cells. Complete mechanistic understanding of how these two functions are implemented within one and the same transport machine has not been attained to date. Based on several lines of structural evidence, a hypothesis was proposed postulating that NPCs shares common evolutionary origin with other intracellular systems responsible for active management of endomembranes...
May 1, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28472469/piwi-interacts-with-chromatin-at-nuclear-pores-and-promiscuously-binds-nuclear-transcripts-in-drosophila-ovarian-somatic-cells
#9
Artem A Ilyin, Sergei S Ryazansky, Semen A Doronin, Oxana M Olenkina, Elena A Mikhaleva, Evgeny Y Yakushev, Yuri A Abramov, Stepan N Belyakin, Anton V Ivankin, Alexey V Pindyurin, Vladimir A Gvozdev, Mikhail S Klenov, Yuri Y Shevelyov
Piwi in a complex with Piwi-interacting RNAs (piRNAs) triggers transcriptional silencing of transposable elements (TEs) in Drosophila ovaries, thus ensuring genome stability. To do this, Piwi must scan the nascent transcripts of genes and TEs for complementarity to piRNAs. The mechanism of this scanning is currently unknown. Here we report the DamID-seq mapping of multiple Piwi-interacting chromosomal domains in somatic cells of Drosophila ovaries. These domains significantly overlap with genomic regions tethered to Nuclear Pore Complexes (NPCs)...
May 2, 2017: Nucleic Acids Research
https://www.readbyqxmd.com/read/28463551/comparative-interactomics-provides-evidence-for-functional-specialization-of-the-nuclear-pore-complex
#10
Samson O Obado, Mark C Field, Michael P Rout
The core architecture of the eukaryotic cell was established well over one billion years ago, and is largely retained in all extant lineages. However, eukaryotic cells also possess lineage-specific features, frequently keyed to specific functional requirements. One quintessential core eukaryotic structure is the nuclear pore complex (NPC), responsible for regulating exchange of macromolecules between the nucleus and cytoplasm as well as acting as a nuclear organizational hub. NPC architecture has been best documented in one eukaryotic supergroup, the Opisthokonts (e...
May 2, 2017: Nucleus
https://www.readbyqxmd.com/read/28455351/the-nucleoporin-nup2-contains-a-meiotic-autonomous-region-that-promotes-the-dynamic-chromosome-events-of-meiosis
#11
Daniel B Chu, Tatiana Gromova, Trent A C Newman, Sean M Burgess
Meiosis is a specialized cellular program required to create haploid gametes from diploid parent cells. Homologous chromosomes pair, synapse, and recombine in a dynamic environment that accommodates gross chromosome reorganization and significant chromosome motion, which are critical for normal chromosome segregation. In Saccharomyces cerevisiae, Ndj1 is a meiotic telomere-associated protein required for physically attaching telomeres to proteins embedded in the nuclear envelope. In this study, we identified additional proteins that act at the nuclear periphery from meiotic cell extracts, including Nup2, a nonessential nucleoporin with a known role in tethering interstitial chromosomal loci to the nuclear pore complex...
April 28, 2017: Genetics
https://www.readbyqxmd.com/read/28451174/reactive-surface-organometallic-complexes-observed-using-dynamic-nuclear-polarization-surface-enhanced-nmr-spectroscopy
#12
Eva Pump, Jasmine Viger-Gravel, Edy Abou-Hamad, Manoja K Samantaray, Bilel Hamzaoui, Andrei Gurinov, Dalaver H Anjum, David Gajan, Anne Lesage, Anissa Bendjeriou-Sedjerari, Lyndon Emsley, Jean-Marie Basset
Dynamic Nuclear Polarization Surface Enhanced NMR Spectroscopy (DNP SENS) is an emerging technique that allows access to high-sensitivity NMR spectra from surfaces. However, DNP SENS usually requires the use of radicals as an exogenous source of polarization, which has so far limited applications for organometallic surface species to those that do not react with the radicals. Here we show that reactive surface species can be studied if they are immobilized inside porous materials with suitably small windows, and if bulky nitroxide bi-radicals (here TEKPol) are used as the polarization source and which cannot enter the pores...
January 1, 2017: Chemical Science
https://www.readbyqxmd.com/read/28446921/roles-of-nuclear-pores-and-nucleo-cytoplasmic-trafficking-in-plant-stress-responses
#13
REVIEW
Yu Yang, Wei Wang, Zhaoqing Chu, Jian-Kang Zhu, Huiming Zhang
The nuclear pore complex (NPC) is a large protein complex that controls the exchange of components between the nucleus and the cytoplasm. In plants, the NPC family components play critical roles not only in essential growth and developmental processes, but also in plant responses to various environmental stress conditions. The involvement of NPC components in plant stress responses is mainly attributed to different mechanisms including control of mRNA/protein nucleo-cytoplasmic trafficking and transcriptional gene regulation...
2017: Frontiers in Plant Science
https://www.readbyqxmd.com/read/28437075/fluorescent-photoswitchable-diarylethenes-for-biolabeling-and-single-molecule-localization-microscopies-with-optical-superresolution
#14
Benoît Roubinet, Michael Weber, Heydar Shojaei, Mark Bates, Mariano L Bossi, Vladimir N Belov, Masahiro Irie, Stefan W Hell
A modular assembly of water-soluble diarylethenes (DAEs), applicable as biomarkers for optical nanoscopy, is reported. Reversibly photoswitchable 1,2-bis(2-alkyl-6-phenyl-1-benzothiophene-1,1-dioxide-3-yl)perfluorocyclopentenes possessing a fluorescent "closed" form were decorated with one or two methoxy group(s) attached to the para-position(s) of phenyl ring(s) and two, four, or eight carboxylic acid groups. Antibody conjugates of these DAEs feature low aggregation, efficient photoswitching in aqueous buffers, specific staining of cellular structures, and photophysical properties (high emission efficiencies and low cycloreversion quantum yields) enabling their application in superresolution microscopy...
May 4, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28435614/time-resolved-biophysical-approaches-to-nucleocytoplasmic-transport
#15
REVIEW
Francesco Cardarelli
Molecules are continuously shuttling across the nuclear envelope barrier that separates the nucleus from the cytoplasm. Instead of being just a barrier to diffusion, the nuclear envelope is rather a complex filter that provides eukaryotes with an elaborate spatiotemporal regulation of fundamental molecular processes, such as gene expression and protein translation. Given the highly dynamic nature of nucleocytoplasmic transport, during the past few decades large efforts were devoted to the development and application of time resolved, fluorescence-based, biophysical methods to capture the details of molecular motion across the nuclear envelope...
2017: Computational and Structural Biotechnology Journal
https://www.readbyqxmd.com/read/28421749/design-of-multifunctional-nanogate-in-response-to-multiple-external-stimuli-using-amphiphilic-diblock-copolymer
#16
Kai Huang, Igal Szleifer
Nature uses the interplay between hydrophobic and electrostatic interactions of disordered proteins to orchestrate complicated molecular gates such as the nuclear pore complex to control the transport of biological masses. Inspired by nature, we here theoretically show that well-defined gate shape, sensitive response to pH and salt concentration, and selectivity in cargo transport can be simultaneously achieved by grafting amphiphilic diblock copolymers made of sequence-controlled hydrophobic and ionizable monomers on the inner surface of solid-state nanopore...
April 28, 2017: Journal of the American Chemical Society
https://www.readbyqxmd.com/read/28408483/o-glcnac-cycling-and-the-regulation-of-nucleocytoplasmic-dynamics
#17
REVIEW
Moriah Eustice, Michelle R Bond, John A Hanover
The dynamic carbohydrate post-translational modification (PTM) O-linked β-N-acetyl glucosamine (O-GlcNAc) is found on thousands of proteins throughout the nucleus and cytoplasm, and rivals phosphorylation in terms of the number of substrates and pathways influenced. O-GlcNAc is highly conserved and essential in most organisms, with disruption of O-GlcNAc cycling linked to diseases ranging from cancer to neurodegeneration. Nuclear pore proteins were the first identified O-GlcNAc-modified substrates, generating intense and ongoing interest in understanding the role of O-GlcNAc cycling in nuclear pore complex structure and function...
April 15, 2017: Biochemical Society Transactions
https://www.readbyqxmd.com/read/28406021/the-nup62-coiled-coil-motif-provides-plasticity-for-triple-helix-bundle-formation
#18
Pravin S Dewangan, Parshuram J Sonawane, Ankita R Chouksey, Radha Chauhan
The central transport channel of the vertebrate nuclear pore complex (NPC) consists of nucleoporins: Nup62, Nup54, and Nup58. The coiled-coil domains in α-helical regions of these nucleoporins are thought to be crucial for several protein-protein interactions in the NPC subcomplexes. In this study, we determined the crystal structure of the coiled-coil domain of rat Nup62 fragment (residues 362-425) to 2.4 Å resolution. The crystal structure shows the conserved coiled-coil domain as a parallel three-helix bundle for the Nup62(362-425) fragment...
April 26, 2017: Biochemistry
https://www.readbyqxmd.com/read/28402725/visualization-of-pml-nuclear-import-complexes-reveals-fg-repeat-nucleoporins-at-cargo-retrieval-sites
#19
Anna Lång, Jens Eriksson, Kay Oliver Schink, Emma Lång, Pernille Blicher, Anna Połeć, Andreas Brech, Bjørn Dalhus, Stig Ove Bøe
Selective nuclear import in eukaryotic cells involves sequential interactions between nuclear import receptors and phenylalanine-glycine (FG)-repeat nucleoporins. Traditionally, binding of cargoes to import receptors is perceived as a nuclear pore complex independent event, while interactions between import complexes and nucleoporins are thought to take place at the nuclear pores. However, studies have shown that nucleoporins are mobile and not static within the nuclear pores, suggesting that they may become engaged in nuclear import before nuclear pore entry...
April 12, 2017: Nucleus
https://www.readbyqxmd.com/read/28398483/function-of-nuclear-membrane-proteins-in-shaping-the-nuclear-envelope-integrity-during-closed-mitosis
#20
Hui-Ju Yang, Masaaki Iwamoto, Yasushi Hiraoka, Tokuko Haraguchi
The nuclear envelope (NE) not only protects the genome from being directly accessed by detrimental agents but also regulates genome organization. Breaches in NE integrity threaten genome stability and impede cellular function. Nonetheless, the NE constantly remodels, and NE integrity is endangered in dividing or differentiating cells. Specifically, in unicellular eukaryotes undergoing closed mitosis, the NE expands instead of breaking down during chromosome segregation. The newly assembling nuclear pore complexes (NPCs) penetrate the existing NE in interphase...
June 1, 2017: Journal of Biochemistry
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