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Nuclear pore complex

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https://www.readbyqxmd.com/read/28821644/calpain-dependent-degradation-of-nucleoporins-contributes-to-motor-neuron-death-in-a-mouse-model-of-chronic-excitotoxicity
#1
Kaori Sugiyama, Tomomi Aida, Masatoshi Nomura, Ryoichi Takayanagi, Hanns U Zeilhofer, Kohichi Tanaka
Glutamate-mediated excitotoxicity induces neuronal death by altering various intracellular signaling pathways and is implicated as a common pathogenic pathway in many neurodegenerative diseases. In the case of motor neuron disease, there is significant evidence to suggest that overactivation of AMPA receptors due to deficiencies in the expression and function of glial glutamate transporter GLT1 and GLAST plays an important role in the mechanisms of neuronal death. However, a causal role for glial glutamate transporter dysfunction in motor neuron death remains unknown...
August 16, 2017: Journal of Neuroscience: the Official Journal of the Society for Neuroscience
https://www.readbyqxmd.com/read/28811369/obesity-associated-gene-tmem18-has-a-role-in-the-central-control-of-appetite-and-body-weight-regulation
#2
Rachel Larder, M F Michelle Sim, Pawan Gulati, Robin Antrobus, Y C Loraine Tung, Debra Rimmington, Eduard Ayuso, Joseph Polex-Wolf, Brian Y H Lam, Cristina Dias, Darren W Logan, Sam Virtue, Fatima Bosch, Giles S H Yeo, Vladimir Saudek, Stephen O'Rahilly, Anthony P Coll
An intergenic region of human chromosome 2 (2p25.3) harbors genetic variants which are among those most strongly and reproducibly associated with obesity. The gene closest to these variants is TMEM18, although the molecular mechanisms mediating these effects remain entirely unknown. Tmem18 expression in the murine hypothalamic paraventricular nucleus (PVN) was altered by changes in nutritional state. Germline loss of Tmem18 in mice resulted in increased body weight, which was exacerbated by high fat diet and driven by increased food intake...
August 15, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28803731/purification-and-characterization-of-the-colicin-a-immunity-protein-in-detergent-micelles
#3
Ane Metola, Ana M Bouchet, Marian Alonso-Mariño, Tammo Diercks, Lena Mäler, Félix M Goñi, Ana R Viguera
The immunity proteins against pore-forming colicins represent a family of integral membrane proteins that reside in the inner membrane of producing cells. Cai, the colicin A immunity protein, was characterized here in detergent micelles by circular dichroism (CD), size exclusion chromatography, chemical cross-linking, nuclear magnetic resonance (NMR) spectroscopy, cysteine accessibility, and colicin A binding in detergent micelles. Bile-salt derivatives induced extensive protein polymerization that precluded further investigation...
August 10, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28791779/crystal-structure-of-the-xpo1p-nuclear-export-complex-bound-to-the-sxfg-pxfg-repeats-of-the-nucleoporin-nup42p
#4
Masako Koyama, Hidemi Hirano, Natsuki Shirai, Yoshiyuki Matsuura
Xpo1p (yeast CRM1) is the major nuclear export receptor that carries a plethora of proteins and ribonucleoproteins from the nucleus to cytoplasm. The passage of the Xpo1p nuclear export complex through nuclear pore complexes (NPCs) is facilitated by interactions with nucleoporins (Nups) containing extensive repeats of phenylalanine-glycine (so-called FG repeats), although the precise role of each Nup in the nuclear export reaction remains incompletely understood. Here we report structural and biochemical characterization of the interactions between the Xpo1p nuclear export complex and the FG repeats of Nup42p, a nucleoporin localized at the cytoplasmic face of yeast NPCs and has characteristic SxFG/PxFG sequence repeat motif...
August 8, 2017: Genes to Cells: Devoted to Molecular & Cellular Mechanisms
https://www.readbyqxmd.com/read/28747499/effects-of-the-inner-nuclear-membrane-proteins-sun1-unc-84a-and-sun2-unc-84b-on-the-early-steps-of-hiv-1-infection
#5
Torsten Schaller, Lorenzo Bulli, Darja Pollpeter, Gilberto Betancor, Juliane Kutzner, Luis Apolonia, Nikolas Herold, Robin Burk, Michael H Malim
Human immunodeficiency virus type 1 (HIV-1) infection of dividing and non-dividing cells involves regulatory interactions with the nuclear pore complex (NPC), followed by translocation to the nucleus and preferential integration into genomic areas in proximity to the inner nuclear membrane (INM). To identify host proteins that may contribute to these processes, we performed an overexpression screen of known membrane-associated NE proteins. We found that the integral transmembrane proteins SUN1/UNC84A and SUN2/UNC84B are potent or modest inhibitors of HIV-1 infection, respectively, and that suppression corresponds to defects in the accumulation of viral cDNA in the nucleus...
July 26, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28747316/mitotic-nuclear-pore-complex-segregation-involves-nup2-in-aspergillus-nidulans
#6
Subbulakshmi Suresh, Sarine Markossian, Aysha H Osmani, Stephen A Osmani
Transport through nuclear pore complexes (NPCs) during interphase is facilitated by the nucleoporin Nup2 via its importin α- and Ran-binding domains. However, Aspergillus nidulans and vertebrate Nup2 also locate to chromatin during mitosis, suggestive of mitotic functions. In this study, we report that Nup2 is required for mitotic NPC inheritance in A. nidulans Interestingly, the role of Nup2 during mitotic NPC segregation is independent of its importin α- and Ran-binding domains but relies on a central targeting domain that is necessary for localization and viability...
July 26, 2017: Journal of Cell Biology
https://www.readbyqxmd.com/read/28734734/nuclear-pore-complexes-a-scaffold-regulating-developmental-transcription
#7
Atsushi Satomura, Jason H Brickner
Nuclear pore complexes (NPCs) have a conserved, but poorly understood, role in transcriptional regulation. Recently, in Developmental Cell, Raices et al. argued that tissue-specific nuclear pore proteins (Nups) act as scaffolds that recruit the transcription factor Mef2C to the NPC, promoting transcription of NPC-associated genes during muscle development.
September 2017: Trends in Cell Biology
https://www.readbyqxmd.com/read/28734076/ensemble-characterization-of-an-intrinsically-disordered-fg-nup-peptide-and-its-f-a-mutant-in-dmso-d6
#8
Korey M Reid, Punnepalli Sunanda, S Raghothama, V V Krishnan
Intrinsically disordered proteins (IDP) lack a well-defined 3D-structure under physiological conditions, yet, the inherent disorder represented by an ensemble of conformation plays a critical role in many cellular and regulatory processes. Nucleoporins, or Nups, are the proteins found in the nuclear pore complex (NPC). The central pore of the NPC is occupied by Nups, which have phenylalanine-glycine domain repeats and are intrinsically disordered, and therefore are termed FG-Nups. These FG-domain repeats exhibit differing cohesiveness character and differ from least (FG) to most (GLFG) cohesive...
July 22, 2017: Biopolymers
https://www.readbyqxmd.com/read/28731850/the-diagnostic-accuracy-of-biomarkers-for-diagnosis-of-primary-biliary-cholangitis-pbc-in-anti-mitochondrial-antibody-ama-negative-pbc-patients-a-review-of-literature
#9
Federica de Liso, Caterina Matinato, Mariangela Ronchi, Rita Maiavacca
Primary biliary cholangitis (PBC), also known as primary biliary cirrhosis, is an autoimmune disease of the liver characterized by anti-mitochondrial antibodies (AMA) in 90%-95% of patients. The aim of this study was to evaluate the diagnostic value of several serum biomarkers in patients with PBC but negative for AMA. Some antinuclear antibodies (ANA) pattern, detected by indirect immunofluorescence (IIF), such as multiple nuclear dot (MND) and rim-like patterns are well-known to be specific for PBC. The corresponding nuclear antigens are the components of the nuclear pore complex (Gp210 for rim-like pattern) and Sp100, PML proteins (for MND pattern) detectable by immunoblotting and ELISA methods...
July 21, 2017: Clinical Chemistry and Laboratory Medicine: CCLM
https://www.readbyqxmd.com/read/28720791/in-vivo-analysis-of-protein-crowding-within-the-nuclear-pore-complex-in-interphase-and-mitosis
#10
Hide A Konishi, Suguru Asai, Tomonobu M Watanabe, Shige H Yoshimura
The central channel of the nuclear pore complex (NPC) is occupied by non-structured polypeptides with a high content of Phe-Gly (FG) motifs. This protein-rich environment functions as an entropic barrier that prevents the passage of molecules, as well as the binding sites for karyopherins, to regulate macromolecular traffic between the nucleoplasm and the cytoplasm. In this study, we expressed individual Nups fused with a crowding-sensitive probe (GimRET) to determine the spatial distribution of protein-rich domains within the central channel in vivo, and characterize the properties of the entropic barrier...
July 18, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28713609/the-molecular-mechanism-for-nuclear-transport-and-its-application
#11
REVIEW
Yun Hak Kim, Myoung-Eun Han, Sae-Ock Oh
Transportation between the cytoplasm and the nucleoplasm is critical for many physiological and pathophysiological processes including gene expression, signal transduction, and oncogenesis. So, the molecular mechanism for the transportation needs to be studied not only to understand cell physiological processes but also to develop new diagnostic and therapeutic targets. Recent progress in the research of the nuclear transportation (import and export) via nuclear pore complex and four important factors affecting nuclear transport (nucleoporins, Ran, karyopherins, and nuclear localization signals/nuclear export signals) will be discussed...
June 2017: Anatomy & Cell Biology
https://www.readbyqxmd.com/read/28712764/nucleocytoplasmic-transport-in-cells-with-progerin-induced-defective-nuclear-lamina
#12
Gianmarco Ferri, Barbara Storti, Ranieri Bizzarri
Recent data indicate that nuclear lamina (NL) plays a relevant role in many fundamental cellular functions. The peculiar role of NL in cells is dramatically demonstrated by the Hutchinson-Gilford progeria syndrome (HGPS), an inherited laminopathy that causes premature, rapid aging shortly after birth. In HGPS, a mutant form of Lamin A (progeria) leads to a dysmorphic NL structure, but how this perturbation is transduced into cellular changes is still largely unknown. Owing to the close structural relationship between NL and the Nuclear Pore Complex (NPC), in this work we test whether HGPS affects passive and active nucleo-cytoplasmic shuttling of cargoes by means of an established model based of fluorescence recovery after photobleaching...
June 28, 2017: Biophysical Chemistry
https://www.readbyqxmd.com/read/28711524/strategic-disruption-of-nuclear-pores-structure-integrity-and-barrier-for-nuclear-apoptosis
#13
REVIEW
Victor Shahin
Apoptosis is a programmed cell death playing key roles in physiology and pathophysiology of multi cellular organisms. Its nuclear manifestation requires transmission of the death signals across the nuclear pore complexes (NPCs). In strategic sequential steps apoptotic factors disrupt NPCs structure, integrity and barrier ultimately leading to nuclear breakdown. The present review reflects on these steps.
July 12, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28700925/protein-transport-by-the-nuclear-pore-complex-simple-biophysics-of-a-complex-biomachine
#14
REVIEW
Tijana Jovanovic-Talisman, Anton Zilman
In eukaryotic cells, transport of molecules between the nucleus and the cytoplasm is facilitated by highly selective and efficient biomachines known as nuclear pore complexes (NPCs). The structural details of NPCs vary across species, with many of their constituent proteins exhibiting relatively low sequence conservation; yet the NPC as a whole retains its general architecture and mechanism of action in all eukaryotes from yeast to humans. This functional conservation in the absence of precise molecular conservation suggests that many aspects of the NPC transport mechanism may be understood based on general biophysical considerations...
July 11, 2017: Biophysical Journal
https://www.readbyqxmd.com/read/28696859/nucleoporins-redistribute-inside-the-nucleus-after-cell-cycle-arrest-induced-by-histone-deacetylases-inhibition
#15
Miguel Pérez-Garrastachu, Jon Arluzea, Ricardo Andrade, Alejandro Díez-Torre, Marta Urtizberea, Margarita Silió, Juan Aréchaga
Nucleoporins are the main components of the nuclear-pore complex (NPC) and were initially considered as mere structural elements embedded in the nuclear envelope, being responsible for nucleocytoplasmic transport. Nevertheless, several recent scientific reports have revealed that some nucleoporins participate in nuclear processes such as transcription, replication, DNA repair and chromosome segregation. Thus, the interaction of NPCs with chromatin could modulate the distribution of chromosome territories relying on the epigenetic state of DNA...
July 11, 2017: Nucleus
https://www.readbyqxmd.com/read/28676424/nuclear-pore-complex-tethers-to-the-cytoskeleton
#16
REVIEW
Martin W Goldberg
The nuclear envelope is tethered to the cytoskeleton. The best known attachments of all elements of the cytoskeleton are via the so-called LINC complex. However, the nuclear pore complexes, which mediate the transport of soluble and membrane bound molecules, are also linked to the microtubule network, primarily via motor proteins (dynein and kinesins) which are linked, most importantly, to the cytoplasmic filament protein of the nuclear pore complex, Nup358, by the adaptor BicD2. The evidence for such linkages and possible roles in nuclear migration, cell cycle control, nuclear transport and cell architecture are discussed...
July 1, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28676422/kinetics-of-transport-through-the-nuclear-pore-complex
#17
REVIEW
Ulrich Kubitscheck, Jan-Peter Siebrasse
Single molecule microscopy techniques allow to visualize the translocation of single transport receptors and cargo molecules or particles through nuclear pore complexes. These data indicate that cargo molecule import into the nucleus takes less than 10ms and nuclear export of messenger RNA (mRNA) particles takes 50-350ms, up to several seconds for extremely bulky particles. This review summarizes and discusses experimental results on transport of nuclear transport factor 2 (NTF2), importin β and mRNA particles...
July 1, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28673770/alterations-of-the-nuclear-transport-system-in-hepatocellular-carcinoma-new-basis-for-therapeutic-strategies
#18
REVIEW
Martin Beck, Peter Schirmacher, Stephan Singer
Hepatocellular carcinoma (HCC) is among the most prevalent human malignancies world-wide with rising incidence in industrialized countries, few therapeutic options and poor prognosis. To expand and improve therapeutic strategies identification of drug targets ideally involved in several liver cancer relevant pathways appears mandatory. Virtually all signal transduction cascades cross the nuclear envelope and thereby require components of the nuclear transport system (NTS) including nuclear transport receptors (e...
June 30, 2017: Journal of Hepatology
https://www.readbyqxmd.com/read/28669824/floppy-but-not-sloppy-interaction-mechanism-of-fg-nucleoporins-and-nuclear-transport-receptors
#19
REVIEW
Iker Valle Aramburu, Edward A Lemke
The nuclear pore complex (NPC) forms a permeability barrier between the nucleus and the cytoplasm. Molecules that are able to cross this permeability barrier encounter different disordered phenylalanine glycine rich nucleoporins (FG-Nups) that act as a molecular filter and regulate the selective NPC crossing of biomolecules. In this review, we provide a current overview regarding the interaction mechanism between FG-Nups and the carrier molecules that recognize and enable the transport of cargoes through the NPC aiming to understand the general molecular mechanisms that facilitate the nucleocytoplasmic transport...
June 30, 2017: Seminars in Cell & Developmental Biology
https://www.readbyqxmd.com/read/28659328/characterization-of-spindle-pole-body-duplication-reveals-a-regulatory-role-for-nuclear-pore-complexes
#20
Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, Elmar Schiebel
The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures...
August 7, 2017: Journal of Cell Biology
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