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Nuclear pore complex

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https://www.readbyqxmd.com/read/28088069/nuclear-pore-complexes-and-regulation-of-gene-expression
#1
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
#2
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
#3
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...
January 9, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28069555/self-assembled-protein-nanocarrier-for-intracellular-delivery-of-antibody
#4
Sung In Lim, Cyril I Lukianov, Julie A Champion
Despite the great potential of antibodies as intracellular therapeutics, there is a significant, unmet challenge in delivering sufficient amounts of folded antibodies inside cells. We describe an all-protein self-assembled nanocarrier capable of delivering functional antibodies to the cytosol. By combining an α-helical peptide that self-assembles into a hexameric coiled-coil bundle and an Fc-binding Protein A fragment, we generated the Hex nanocarrier that is efficiently internalized by cells without cytotoxicity...
January 6, 2017: Journal of Controlled Release: Official Journal of the Controlled Release Society
https://www.readbyqxmd.com/read/28068389/cooperative-interactions-between-different-classes-of-disordered-proteins-play-a-functional-role-in-the-nuclear-pore-complex-of-baker-s-yeast
#5
David Ando, Ajay Gopinathan
Nucleocytoplasmic transport is highly selective, efficient, and is regulated by a poorly understood mechanism involving hundreds of disordered FG nucleoporin proteins (FG nups) lining the inside wall of the nuclear pore complex (NPC). Previous research has concluded that FG nups in Baker's yeast (S. cerevisiae) are present in a bimodal distribution, with the "Forest Model" classifying FG nups as either di-block polymer like "trees" or single-block polymer like "shrubs". Using a combination of coarse-grained modeling and polymer brush modeling, the function of the di-block FG nups has previously been hypothesized in the Di-block Copolymer Brush Gate (DCBG) model to form a higher-order polymer brush architecture which can open and close to regulate transport across the NPC...
2017: PloS One
https://www.readbyqxmd.com/read/28062321/tom9-2-is-a-calmodulin-binding-protein-critical-for-tom-complex-assembly-but-not-for-mitochondrial-protein-import-in-arabidopsis-thaliana
#6
Nargis Parvin, Chris Carrie, Isabelle Pabst, Antonia Läßer, Debabrata Laha, Melanie Paul, Peter Geigenberger, Ralf Heermann, Kirsten Jung, Ute C Vothknecht, Fatima Chigri
The translocon on the outer membrane of mitochondria (TOM) facilitates import of nuclear encoded proteins. The principal machinery seems conserved in eukaryotes, however, divergence in composition and structure of TOM components has been observed between mammals, yeast and plants. TOM9, the plant homologue of yeast Tom22, is significantly smaller due to a truncation in the cytosolic receptor domain and its precise function is not understood. Here we provide evidences that TOM9.2 from Arabidopsis thaliana is involved in the formation of the mature TOM complex, most likely by influencing the assembly of the pore-forming subunit TOM40...
January 3, 2017: Molecular Plant
https://www.readbyqxmd.com/read/28059701/structural-and-biochemical-analyses-of-the-dead-box-atpase-sub2-in-association-with-tho-or-yra1
#7
Yi Ren, Philip Schmiege, Günter Blobel
mRNA is cotranscrptionally processed and packaged into messenger ribonucleoprotein particles (mRNPs) in the nucleus. Prior to export through the nuclear pore, mRNPs undergo several obligatory remodeling reactions. In yeast, one of these reactions involves loading of the mRNA-binding protein Yra1 by the DEAD-box ATPase Sub2 as assisted by the hetero-pentameric THO complex. To obtain molecular insights into reaction mechanisms, we determined crystal structures of two relevant complexes: a THO hetero-pentamer bound to Sub2 at 6...
January 6, 2017: ELife
https://www.readbyqxmd.com/read/28057257/have-nec-coat-will-travel-structural-basis-of-membrane-budding-during-nuclear-egress-in-herpesviruses
#8
REVIEW
J M Bigalke, E E Heldwein
Herpesviruses are unusual among enveloped viruses because they bud twice yet acquire a single envelope. Furthermore, unlike other DNA viruses that replicate in the nucleus, herpesviruses do not exit it by passing through the nuclear pores or by rupturing the nuclear envelope. Instead, herpesviruses have a complex mechanism of nuclear escape whereby nascent capsids bud at the inner nuclear membrane to form perinuclear virions that subsequently fuse with the outer nuclear membrane, releasing capsids into the cytosol...
2017: Advances in Virus Research
https://www.readbyqxmd.com/read/28054750/somatic-med12-nonsense-mutation-escapes-mrna-decay-and-reveals-a-motif-required-for-nuclear-entry
#9
Tuomas Heikkinen, Kati Kämpjärvi, Salla Keskitalo, Pernilla von Nandelstadh, Xiaonan Liu, Ville Rantanen, Esa Pitkänen, Matias Kinnunen, Heikki Kuusanmäki, Mika Kontro, Mikko Turunen, Netta Mäkinen, Jussi Taipale, Caroline Heckman, Kaisa Lehti, Satu Mustjoki, Markku Varjosalo, Pia Vahteristo
MED12 is a key component of the transcription-regulating Mediator complex. Specific missense and in-frame insertion/deletion mutations in exons 1 and 2 have been identified in uterine leiomyomas, breast tumors, and chronic lymphocytic leukemia. Here, we characterize the first MED12 5' end nonsense mutation (c.97G>T, p.E33X) identified in acute lymphoblastic leukemia and show that it escapes nonsense-mediated mRNA decay (NMD) by using an alternative translation initiation site. The resulting N-terminally truncated protein is unable to enter the nucleus due to the lack of identified nuclear localization signal (NLS)...
January 5, 2017: Human Mutation
https://www.readbyqxmd.com/read/28045133/calpain-dependent-disruption-of-nucleo-cytoplasmic-transport-in-als-motor-neurons
#10
Takenari Yamashita, Hitoshi Aizawa, Sayaka Teramoto, Megumi Akamatsu, Shin Kwak
Nuclear dysfunction in motor neurons has been hypothesized to be a principal cause of amyotrophic lateral sclerosis (ALS) pathogenesis. Here, we investigated the mechanism by which the nuclear pore complex (NPC) is disrupted in dying motor neurons in a mechanistic ALS mouse model (adenosine deaminase acting on RNA 2 (ADAR2) conditional knockout (AR2) mice) and in ALS patients. We showed that nucleoporins (Nups) that constituted the NPC were cleaved by activated calpain via a Ca(2+)-permeable AMPA receptor-mediated mechanism in dying motor neurons lacking ADAR2 expression in AR2 mice...
January 3, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28039207/nup358-binds-to-ago-proteins-through-its-sumo-interacting-motifs-and-promotes-the-association-of-target-mrna-with-mirisc
#11
Manas Ranjan Sahoo, Swati Gaikwad, Deepak Khuperkar, Maitreyi Ashok, Mary Helen, Santosh Kumar Yadav, Aditi Singh, Indrasen Magre, Prachi Deshmukh, Supriya Dhanvijay, Pabitra Kumar Sahoo, Yogendra Ramtirtha, Mallur Srivatsan Madhusudhan, Pananghat Gayathri, Vasudevan Seshadri, Jomon Joseph
MicroRNA (miRNA)-guided mRNA repression, mediated by the miRNA-induced silencing complex (miRISC), is an important component of post-transcriptional gene silencing. However, how miRISC identifies the target mRNA in vivo is not well understood. Here, we show that the nucleoporin Nup358 plays an important role in this process. Nup358 localizes to the nuclear pore complex and to the cytoplasmic annulate lamellae (AL), and these structures dynamically associate with two mRNP granules: processing bodies (P bodies) and stress granules (SGs)...
December 30, 2016: EMBO Reports
https://www.readbyqxmd.com/read/28035044/a-role-for-gle1-a-regulator-of-dead-box-rna-helicases-at-centrosomes-and-basal-bodies
#12
Li-En Jao, Abdalla Akef, Susan R Wente
Control of organellar assembly and function is critical to eukaryotic homeostasis and survival. Gle1 is a highly conserved regulator of RNA-dependent DEAD-box ATPase proteins, with critical roles in both mRNA export and translation. In addition to its well-defined interaction with nuclear pore complexes, here we find that Gle1 is enriched at the centrosome and basal body. Gle1 assembles into the toroid-shaped pericentriolar material around the mother centriole. Reduced Gle1 levels are correlated with decreased pericentrin localization at the centrosome and microtubule organization defects...
January 1, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28033038/mgo3-and-gip1-act-synergistically-for-the-maintenance-of-centromeric-cohesion
#13
Morgane Batzenschlager, Anne-Catherine Schmit, Etienne Herzog, Joerg Fuchs, Veit Schubert, Guy Houlné, Marie-Edith Chabouté
The control of genomic maintenance during S phase is crucial in eukaryotes. It involves the establishment of sister chromatid cohesion, ensuring faithful chromosome segregation, as well as proper DNA replication and repair to preserve genetic information. In animals, nuclear periphery proteins - including inner nuclear membrane proteins and nuclear pore-associated components - are key factors which regulate DNA integrity. Corresponding functional homologues are not so well known in plants which may have developed specific mechanisms due to their sessile life...
December 29, 2016: Nucleus
https://www.readbyqxmd.com/read/28029704/dynamic-mislocalizations-of-nuclear-pore-complex-proteins-after-focal-cerebral-ischemia-in-rat
#14
Qian Li, Yasuyuki Ohta, Toru Yamashita, Jingwei Shang, Kentaro Deguchi, Tian Feng, Kota Sato, Nozomi Hishikawa, Yumiko Nakano, Koji Abe
Nuclear pore complexes (NPCs) play an important role in coordinating the transport of proteins and nucleic acids between the nucleus and cytoplasm, and are therefore essential for maintaining normal cellular function and liability. In the present study, we investigated the temporal immunohistochemical distribution of five representative components of NPCs-Ran GTPase-activating protein 1 (RanGap1), glycoprotein-210 (Gp210), nucleoporin 205 (Nup205), nucleoporin 107 (Nup107), and nucleoporin 50 (Nup50)-after 90 min of transient middle cerebral artery occlusion (tMCAO) up to 28 days after the reperfusion in rat brains...
December 28, 2016: Journal of Neuroscience Research
https://www.readbyqxmd.com/read/28000054/5-flurouracil-disrupts-nuclear-export-and-nuclear-pore-permeability-in-a-calcium-dependent-manner
#15
Kelly J Higby, Melissa M Bischak, Christina A Campbell, Rebecca G Anderson, Sarah A Broskin, Lauren E Foltz, Jarrett A Koper, Audrey C Nickle, Karen K Resendes
Regulation of nuclear transport is an essential component of apoptosis. As chemotherapy induced cell death progresses, nuclear transport and the nuclear pore complex (NPC) are slowly disrupted and dismantled. 5-Fluorouracil (5-FU) and the camptothecin derivatives irinotecan and topotecan, are linked to altered nuclear transport of specific proteins; however, their general effects on the NPC and transport during apoptosis have not been characterized. We demonstrate that 5-FU, but not topotecan, increases NPC permeability, and disrupts Ran-mediated nuclear transport before the disruption of the NPC...
December 20, 2016: Apoptosis: An International Journal on Programmed Cell Death
https://www.readbyqxmd.com/read/27999437/the-nuclear-pore-complex-understanding-its-function-through-structural-insight
#16
Martin Beck, Ed Hurt
Nuclear pore complexes (NPCs) fuse the inner and outer nuclear membranes to form channels across the nuclear envelope. They are large macromolecular assemblies with a complex composition and diverse functions. Apart from facilitating nucleocytoplasmic transport, NPCs are involved in chromatin organization, the regulation of gene expression and DNA repair. Understanding the molecular mechanisms underlying these functions has been hampered by a lack of structural knowledge about the NPC. The recent convergence of crystallographic and biochemical in vitro analysis of nucleoporins (NUPs), the components of the NPC, with cryo-electron microscopic imaging of the entire NPC in situ has provided first pseudo-atomic view of its central core and revealed that an unexpected network of short linear motifs is an important spatial organization principle...
December 21, 2016: Nature Reviews. Molecular Cell Biology
https://www.readbyqxmd.com/read/27984722/an-ancient-unified-mechanism-for-metformin-growth-inhibition-in-c-%C3%A2-elegans-and-cancer
#17
Lianfeng Wu, Ben Zhou, Noriko Oshiro-Rapley, Man Li, Joao A Paulo, Christopher M Webster, Fan Mou, Michael C Kacergis, Michael E Talkowski, Christopher E Carr, Steven P Gygi, Bin Zheng, Alexander A Soukas
Metformin has utility in cancer prevention and treatment, though the mechanisms for these effects remain elusive. Through genetic screening in C. elegans, we uncover two metformin response elements: the nuclear pore complex (NPC) and acyl-CoA dehydrogenase family member-10 (ACAD10). We demonstrate that biguanides inhibit growth by inhibiting mitochondrial respiratory capacity, which restrains transit of the RagA-RagC GTPase heterodimer through the NPC. Nuclear exclusion renders RagC incapable of gaining the GDP-bound state necessary to stimulate mTORC1...
December 15, 2016: Cell
https://www.readbyqxmd.com/read/27940554/rna-helicase-ddx19-stabilizes-ribosomal-elongation-and-termination-complexes
#18
Tatiana Mikhailova, Ekaterina Shuvalova, Alexander Ivanov, Denis Susorov, Alexey Shuvalov, Peter M Kolosov, Elena Alkalaeva
The human DEAD-box RNA-helicase DDX19 functions in mRNA export through the nuclear pore complex. The yeast homolog of this protein, Dbp5, has been reported to participate in translation termination. Using a reconstituted mammalian in vitro translation system, we show that the human protein DDX19 is also important for translation termination. It is associated with the fraction of translating ribosomes. We show that DDX19 interacts with pre-termination complexes (preTCs) in a nucleotide-dependent manner. Furthermore, DDX19 increases the efficiency of termination complex (TC) formation and the peptide release in the presence of eukaryotic release factors...
December 9, 2016: Nucleic Acids Research
https://www.readbyqxmd.com/read/27939291/structures-of-the-karyopherins-kap121p-and-kap60p-bound-to-the-nuclear-pore-targeting-domain-of-the-sumo-protease-ulp1p
#19
Hidemi Hirano, Junya Kobayashi, Yoshiyuki Matsuura
The budding yeast small ubiquitin-like modifier (SUMO) protease Ulp1p catalyzes both the processing of newly synthesized SUMO to its mature form and the deconjugation of SUMO from target proteins, thereby regulating a wide range of cellular processes including cell division, DNA repair, DNA replication, transcription, and mRNA quality control. Ulp1p is localized primarily at the nuclear pore complex (NPC) through interactions involving the karyopherins Kap121p and Kap95p-Kap60p heterodimer and a subset of nuclear pore-associated proteins...
December 6, 2016: Journal of Molecular Biology
https://www.readbyqxmd.com/read/27935478/labeling-proteins-inside-living-cells-using-external-fluorophores-for-microscopy
#20
Kai Wen Teng, Yuji Ishitsuka, Pin Ren, Yeoan Youn, Xiang Deng, Pinghua Ge, Andrew S Belmont, Paul R Selvin
Site-specific fluorescent labeling of proteins inside live mammalian cells has been achieved by employing Streptolysin O, a bacterial enzyme which forms temporary pores in the membrane and allows delivery of virtually any fluorescent probes, ranging from labeled IgG's to small ligands, with high efficiency (>85% of cells). The whole process, including recovery, takes 30 min, and the cell is ready to be imaged immediately. A variety of cell viability tests were performed after treatment with SLO to ensure that the cells have intact membranes, are able to divide, respond normally to signaling molecules, and maintains healthy organelle morphology...
December 9, 2016: ELife
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