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Nuclear pore complex

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https://www.readbyqxmd.com/read/28314893/integration-of-mrnp-formation-and-export
#1
REVIEW
Petra Björk, Lars Wieslander
Expression of protein-coding genes in eukaryotes relies on the coordinated action of many sophisticated molecular machineries. Transcription produces precursor mRNAs (pre-mRNAs) and the active gene provides an environment in which the pre-mRNAs are processed, folded, and assembled into RNA-protein (RNP) complexes. The dynamic pre-mRNPs incorporate the growing transcript, proteins, and the processing machineries, as well as the specific protein marks left after processing that are essential for export and the cytoplasmic fate of the mRNPs...
March 17, 2017: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/28289229/persistence-of-the-mitochondrial-permeability-transition-in-the-absence-of-subunit-c-of-human-atp-synthase
#2
Jiuya He, Holly C Ford, Joe Carroll, Shujing Ding, Ian M Fearnley, John E Walker
The permeability transition in human mitochondria refers to the opening of a nonspecific channel, known as the permeability transition pore (PTP), in the inner membrane. Opening can be triggered by calcium ions, leading to swelling of the organelle, disruption of the inner membrane, and ATP synthesis, followed by cell death. Recent proposals suggest that the pore is associated with the ATP synthase complex and specifically with the ring of c-subunits that constitute the membrane domain of the enzyme's rotor...
March 13, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28242692/lem2-recruits-chmp7-for-escrt-mediated-nuclear-envelope-closure-in-fission-yeast-and-human-cells
#3
Mingyu Gu, Dollie LaJoie, Opal S Chen, Alexander von Appen, Mark S Ladinsky, Michael J Redd, Linda Nikolova, Pamela J Bjorkman, Wesley I Sundquist, Katharine S Ullman, Adam Frost
Endosomal sorting complexes required for transport III (ESCRT-III) proteins have been implicated in sealing the nuclear envelope in mammals, spindle pole body dynamics in fission yeast, and surveillance of defective nuclear pore complexes in budding yeast. Here, we report that Lem2p (LEM2), a member of the LEM (Lap2-Emerin-Man1) family of inner nuclear membrane proteins, and the ESCRT-II/ESCRT-III hybrid protein Cmp7p (CHMP7), work together to recruit additional ESCRT-III proteins to holes in the nuclear membrane...
February 27, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28236735/the-nucleus-keeping-it-together-by-keeping-it-apart
#4
REVIEW
C Patrick Lusk, Megan C King
It has been postulated that the segregation of nucleus and cytoplasm supported the development of increased organismal complexity. For example, separating transcription and translation allows for mRNA splicing, while the sequestration of genomic DNA supports the innate immune system's ability to equate cytoplasmic DNA with pathogens. Consistent with the importance of nucleocytoplasmic compartmentalization in a broad array of cellular processes, defects in maintaining discrete nuclear and cytoplasmic compartments, either due to loss of nuclear pore complex integrity, disrupted nuclear transport or ruptures of the nuclear envelope, lead to cellular dysfunction, cell death and disease...
February 21, 2017: Current Opinion in Cell Biology
https://www.readbyqxmd.com/read/28226231/cell-biology-of-the-plant-nucleus
#5
Iris Meier, Eric J Richards, David E Evans
The eukaryotic nucleus is enclosed by the nuclear envelope, which is perforated by the nuclear pores, the gateways of macromolecular exchange between the nucleoplasm and cytoplasm. The nucleoplasm is organized in a complex three-dimensional fashion that changes over time and in response to stimuli. Within the cell, the nucleus must be viewed as an organelle (albeit a gigantic one) that is a recipient of cytoplasmic forces and capable of morphological and positional dynamics. The most dramatic reorganization of this organelle occurs during mitosis and meiosis...
February 22, 2017: Annual Review of Plant Biology
https://www.readbyqxmd.com/read/28221134/human-nup98-regulates-the-localization-and-activity-of-dexh-d-box-helicase-dhx9
#6
Juliana S Capitanio, Ben Montpetit, Richard W Wozniak
Beyond their role at nuclear pore complexes, some nucleoporins function in the nucleoplasm. One such nucleoporin, Nup98, binds chromatin and regulates gene expression. To gain insight into how Nup98 contributes to this process, we focused on identifying novel binding partners and understanding the significance of these interactions. Here we report on the identification of the DExH/D-box helicase DHX9 as an intranuclear Nup98 binding partner. Various results, including in vitro assays, show that the FG/GLFG region of Nup98 binds to N- and C-terminal regions of DHX9 in an RNA facilitated manner...
February 21, 2017: ELife
https://www.readbyqxmd.com/read/28202688/super-resolution-mapping-of-scaffold-nucleoporins-in-the-nuclear-pore-complex
#7
Jiong Ma, Joseph M Kelich, Samuel L Junod, Weidong Yang
The nuclear pore complex (NPC), composed of ∼30 different nucleoporins (Nups), is one of the largest supramolecular structures in eukaryotic cells. Its octagonal ring-scaffold perforates the nuclear envelope and features a unique molecular machinery that regulates nucleocytoplasmic transport. However, the precise copy number and the spatial location of each Nup in the native NPC remain obscure due to the inherent difficulty of counting and localizing proteins inside the sub-micrometer supramolecular complex...
February 15, 2017: Journal of Cell Science
https://www.readbyqxmd.com/read/28197909/sumo-and-nucleocytoplasmic-transport
#8
Christopher Ptak, Richard W Wozniak
The transport of proteins between the nucleus and cytoplasm occurs through nuclear pore complexes and is facilitated by numerous transport factors. These transport processes are often regulated by post-translational modification or, reciprocally, transport can function to control post-translational modifications through regulated transport of key modifying enzymes. This interplay extends to relationships between nucleocytoplasmic transport and SUMO-dependent pathways. Examples of protein sumoylation inhibiting or stimulating nucleocytoplasmic transport have been documented, both through its effects on the physical properties of cargo molecules and by directly regulating the functions of components of the nuclear transport machinery...
2017: Advances in Experimental Medicine and Biology
https://www.readbyqxmd.com/read/28193881/strong-signal-increase-in-sted-fluorescence-microscopy-by-imaging-regions-of-subdiffraction-extent
#9
Fabian Göttfert, Tino Pleiner, Jörn Heine, Volker Westphal, Dirk Görlich, Steffen J Sahl, Stefan W Hell
Photobleaching remains a limiting factor in superresolution fluorescence microscopy. This is particularly true for stimulated emission depletion (STED) and reversible saturable/switchable optical fluorescence transitions (RESOLFT) microscopy, where adjacent fluorescent molecules are distinguished by sequentially turning them off (or on) using a pattern of light formed as a doughnut or a standing wave. In sample regions where the pattern intensity reaches or exceeds a certain threshold, the molecules are essentially off (or on), whereas in areas where the intensity is lower, that is, around the intensity minima, the molecules remain in the initial state...
February 28, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28187419/dynamics-of-mirna-biogenesis-and-nuclear-transport
#10
Aneesh Kotipalli, Ravikumar Gutti, Chanchal K Mitra
MicroRNAs (miRNAs) are short noncoding RNA sequences ~22 nucleotides in length that play an important role in gene regulation-transcription and translation. The processing of these miRNAs takes place in both the nucleus and the cytoplasm while the final maturation occurs in the cytoplasm. Some mature miRNAs with nuclear localisation signals (NLS) are transported back to the nucleus and some remain in the cytoplasm. The functional roles of these miRNAs are seen in both the nucleus and the cytoplasm. In the nucleus, miRNAs regulate gene expression by binding to the targeted promoter sequences and affect either the transcriptional gene silencing (TGS) or transcriptional gene activation (TGA)...
December 22, 2016: Journal of Integrative Bioinformatics
https://www.readbyqxmd.com/read/28179529/differential-disruption-of-nucleocytoplasmic-trafficking-pathways-by-rhinovirus-2a-proteases
#11
Kelly Watters, Bahar Inankur, Jaye C Gardiner, Jay Warrick, Nathan M Sherer, John Yin, Ann C Palmenberg
The RNA rhinoviruses (RV) encode 2A proteases (2A(pro)) that contribute essential polyprotein processing and host-cell shutoff functions during infection, including the cleavage of Phe/Gly-containing nucleoporin proteins (Nups) within nuclear pore complexes (NPC). Within the 3 RV species, multiple divergent genotypes encode diverse 2A(pro) sequences which act differentially on specific Nups. Since only subsets of Phe/Gly motifs, particularly those within Nup62, Nup98 and Nup153, are recognized by transport receptors (karyopherins) when trafficking large molecular cargos through the NPC, the processing preferences of individual 2A(pro) predict RV genotype-specific targeting of NPC pathways and cargos...
February 8, 2017: Journal of Virology
https://www.readbyqxmd.com/read/28179150/transporter-mediated-nuclear-entry-of-jasmonoyl-isoleucine-is-essential-for-jasmonate-signaling
#12
Qingqing Li, Jian Zheng, Shuaizhang Li, Guanrong Huang, Stephen J Skilling, Lijian Wang, Ling Li, Mengya Li, Lixing Yuan, Pei Liu
To control gene expression directly by hormone concentrations, both animal and plant cells have exploited comparable mechanisms to sense small molecular hormones in nucleus. Whether nuclear entry of these hormones is actively transported or passively diffused, as conventionally postulated, through nuclear pore complex remains enigmatic. Here, we identified and characterized a jasmonate transporter in Arabidopsis thaliana, AtJAT1/ AtABCG16, which exhibits an unexpected dual localization in the nuclear envelope and plasma membrane...
February 4, 2017: Molecular Plant
https://www.readbyqxmd.com/read/28162953/molecular-architecture-of-the-major-membrane-ring-component-of-the-nuclear-pore-complex
#13
Paula Upla, Seung Joong Kim, Parthasarathy Sampathkumar, Kaushik Dutta, Sean M Cahill, Ilan E Chemmama, Rosemary Williams, Jeffrey B Bonanno, William J Rice, David L Stokes, David Cowburn, Steven C Almo, Andrej Sali, Michael P Rout, Javier Fernandez-Martinez
The membrane ring that equatorially circumscribes the nuclear pore complex (NPC) in the perinuclear lumen of the nuclear envelope is composed largely of Pom152 in yeast and its ortholog Nup210 (or Gp210) in vertebrates. Here, we have used a combination of negative-stain electron microscopy, nuclear magnetic resonance, and small-angle X-ray scattering methods to determine an integrative structure of the ∼120 kDa luminal domain of Pom152. Our structural analysis reveals that the luminal domain is formed by a flexible string-of-pearls arrangement of nine repetitive cadherin-like Ig-like domains, indicating an evolutionary connection between NPCs and the cell adhesion machinery...
March 7, 2017: Structure
https://www.readbyqxmd.com/read/28146565/nuclear-pore-like-structures-in-a-compartmentalized-bacterium
#14
Evgeny Sagulenko, Amanda Nouwens, Richard I Webb, Kathryn Green, Benjamin Yee, Garry Morgan, Andrew Leis, Kuo-Chang Lee, Margaret K Butler, Nicholas Chia, Uyen Thi Phuong Pham, Stinus Lindgreen, Ryan Catchpole, Anthony M Poole, John A Fuerst
Planctomycetes are distinguished from other Bacteria by compartmentalization of cells via internal membranes, interpretation of which has been subject to recent debate regarding potential relations to Gram-negative cell structure. In our interpretation of the available data, the planctomycete Gemmata obscuriglobus contains a nuclear body compartment, and thus possesses a type of cell organization with parallels to the eukaryote nucleus. Here we show that pore-like structures occur in internal membranes of G...
2017: PloS One
https://www.readbyqxmd.com/read/28138739/characterization-of-a-nuclear-pore-protein-sheds-light-on-the-roles-and-composition-of-the-toxoplasma-gondii-nuclear-pore-complex
#15
Flavie Courjol, Thomas Mouveaux, Kevin Lesage, Jean-Michel Saliou, Elisabeth Werkmeister, Maurine Bonabaud, Marine Rohmer, Christian Slomianny, Franck Lafont, Mathieu Gissot
The nuclear pore is a key structure in eukaryotes regulating nuclear-cytoplasmic transport as well as a wide range of cellular processes. Here, we report the characterization of the first Toxoplasma gondii nuclear pore protein, named TgNup302, which appears to be the orthologue of the mammalian Nup98-96 protein. We produced a conditional knock-down mutant that expresses TgNup302 under the control of an inducible tetracycline-regulated promoter. Under ATc treatment, a substantial decrease of TgNup302 protein in inducible knock-down (iKD) parasites was observed, causing a delay in parasite proliferation...
January 30, 2017: Cellular and Molecular Life Sciences: CMLS
https://www.readbyqxmd.com/read/28122334/metformin-a-metabolic-modulator
#16
Federico Pietrocola, Guido Kroemer
Recent findings have shed new light on the mechanisms of action through which biguanides exert their anti-aging and cytostatic effects in Caenorhabditis elegans and human cell lines. The drop in energy charge resulting from the metformin mediated inhibition of mitochondrial activity affects the function of the nuclear pore complex, blocks mTOR signaling and enhances the expression of ACAD10. Whether the inhibition of this pathway is truly responsible for the anti-diabetic and cancer effects of the drug in mammals remains to be established...
February 7, 2017: Oncotarget
https://www.readbyqxmd.com/read/28112196/the-kinetochore-dependent-and-independent-formation-of-the-cdc20-mad2-complex-and-its-functions-in-hela-cells
#17
Jianquan Li, Nanmao Dang, Daniel James Wood, Jun-Yong Huang
The mitotic checkpoint complex (MCC) is formed from two sub-complexes of CDC20-MAD2 and BUBR1-BUB3, and current models suggest that it is generated exclusively by the kinetochores after nuclear envelope breakdown (NEBD). However, neither sub-complex has been visualised in vivo, and when and where they are formed during the cell cycle and their response to different SAC conditions remains elusive. Using single cell analysis in HeLa cells, we show that the CDC20-MAD2 complex is cell cycle regulated with a "Bell" shaped profile and peaks at prometaphase...
January 23, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28088069/nuclear-pore-complexes-and-regulation-of-gene-expression
#18
REVIEW
Marcela Raices, Maximiliano A D'Angelo
Nuclear pore complexes (NPCs), are large multiprotein channels that penetrate the nuclear envelope connecting the nucleus to the cytoplasm. Accumulating evidence shows that besides their main role in regulating the exchange of molecules between these two compartments, NPCs and their components also play important transport-independent roles, including gene expression regulation, chromatin organization, DNA repair, RNA processing and quality control, and cell cycle control. Here, we will describe the recent findings about the role of these structures in the regulation of gene expression...
January 11, 2017: Current Opinion in Cell Biology
https://www.readbyqxmd.com/read/28071978/nup82-functions-redundantly-with-nup136-in-a-salicylic-acid-dependent-defense-response-of-arabidopsis-thaliana
#19
Kentaro Tamura, Yoichiro Fukao, Noriyuki Hatsugai, Fumiaki Katagiri, Ikuko Hara-Nishimura
The nuclear pore complex (NPC) comprises more than 30 nucleoporins (Nups). NPC mediates macromolecular trafficking between the nucleoplasm and the cytoplasm, but specific roles of individual Nups are poorly understood in higher plants. Here, we show that the novel nucleoporin unique to angiosperm plants (designated as Nup82) functions in a salicylic acid-dependent defense in a redundant manner with Nup136, which is a component of the nuclear basket in the NPC. Arabidopsis thaliana Nup82 had a similar amino acid sequence to the N-terminal half of Nup136 and a Nup82-GFP fusion was localized on the nuclear envelope...
January 10, 2017: Nucleus
https://www.readbyqxmd.com/read/28069952/toxic-prn-poly-dipeptides-encoded-by-the-c9orf72-repeat-expansion-block-nuclear-import-and-export
#20
Kevin Y Shi, Eiichiro Mori, Zehra F Nizami, Yi Lin, Masato Kato, Siheng Xiang, Leeju C Wu, Ming Ding, Yonghao Yu, Joseph G Gall, Steven L McKnight
The toxic proline:arginine (PRn) poly-dipeptide encoded by the (GGGGCC)n repeat expansion in the C9orf72 form of heritable amyotrophic lateral sclerosis (ALS) binds to the central channel of the nuclear pore and inhibits the movement of macromolecules into and out of the nucleus. The PRn poly-dipeptide binds to polymeric forms of the phenylalanine:glycine (FG) repeat domain, which is shared by several proteins of the nuclear pore complex, including those in the central channel. A method of chemical footprinting was used to characterize labile, cross-β polymers formed from the FG domain of the Nup54 protein...
February 14, 2017: Proceedings of the National Academy of Sciences of the United States of America
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