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https://www.readbyqxmd.com/read/27902702/selective-inhibitor-of-nuclear-export-sine-compounds-alter-new-world-alphavirus-capsid-localization-and-reduce-viral-replication-in-mammalian-cells
#1
Lindsay Lundberg, Chelsea Pinkham, Cynthia de la Fuente, Ashwini Brahms, Nazly Shafagati, Kylie M Wagstaff, David A Jans, Sharon Tamir, Kylene Kehn-Hall
The capsid structural protein of the New World alphavirus, Venezuelan equine encephalitis virus (VEEV), interacts with the host nuclear transport proteins importin α/β1 and CRM1. Novel selective inhibitor of nuclear export (SINE) compounds, KPT-185, KPT-335 (verdinexor), and KPT-350, target the host's primary nuclear export protein, CRM1, in a manner similar to the archetypical inhibitor Leptomycin B. One major limitation of Leptomycin B is its irreversible binding to CRM1; which SINE compounds alleviate because they are slowly reversible...
November 2016: PLoS Neglected Tropical Diseases
https://www.readbyqxmd.com/read/27866280/proteasome-mediated-degradation-of-tyrosine-hydroxylase-triggered-by-its-phosphorylation-a-new-question-as-to-the-intracellular-location-at-which-the-degradation-occurs
#2
REVIEW
Akira Nakashima, Yu Kodani, Yoko S Kaneko, Hiroshi Nagasaki, Akira Ota
Tyrosine hydroxylase (TH) is the rate-limiting enzyme in catecholamine biosynthesis, and its stability is a fundamental factor to maintain the level of the catecholamines in cells. However, the intracellular stability of TH determined by the degradation remains unknown; although the TH molecule phosphorylated at its Ser19 was observed in the nucleus, and the phosphorylation suspected to trigger its proteasome-mediated degradation. Computer-assisted analysis using the cNLS Mapper program predicted that two sequences of nuclear localization signals (NLS) exist in the N-terminus of TH molecule containing the phosphorylation sites Ser19, Ser31, and Ser40 (Pro(9)-Arg(38) and Lys(12)-Ile(42)): the NLS scores indicated that TH could become localized in both nucleus and cytoplasm...
November 19, 2016: Journal of Neural Transmission
https://www.readbyqxmd.com/read/27865090/characterization-of-the-subcellular-localization-and-nuclear-import-molecular-mechanisms-of-herpes-simplex-virus-1-ul2
#3
Mingsheng Cai, Zebin Huang, Zongmin Liao, Tao Chen, Ping Wang, Si Jiang, Daixiong Chen, Tao Peng, Yun Bian, Gengde Hong, Hang Yang, Zhancheng Zeng, Xiaowei Li, Meili Li
As a crucial protein, the herpes simplex virus 1 (HSV-1) tegument component UL2 has been shown to take part in various stages of viral infection, nonetheless, its exact subcellular localization and transport molecular determinants is not well known thus far. In the present study, by using live cells fluorescent microscopy assay, UL2 tagged with enhanced yellow fluorescent protein was transient expressed in live cells and showed a completely nuclear accumulation without the presence of other HSV-1 proteins. Moreover, the nuclear transport of UL2 was characterized to be assisted by multiple transport pathways through Ran-, importin α1-, α5-, α7-, β1- and transportin-1 cellular transport receptors...
November 19, 2016: Biological Chemistry
https://www.readbyqxmd.com/read/27862840/differential-nucleocytoplasmic-shuttling-of-the-nucleoprotein-of-influenza-a-viruses-and-association-with-host-tropism
#4
Jing Li, Weinan Zheng, Lidan Hou, Can Chen, Wenhui Fan, Hongren Qu, Jingwen Jiang, Jinhua Liu, George F Gao, Jiyong Zhou, Lei Sun, Wenjun Liu
The nucleoprotein (NP) of influenza A virus plays a crucial role in virus replication, infectivity, and host adaptation. As a major component of the viral ribonucleoprotein complexes (vRNP), NP initiates vRNP shuttling between the nucleus and cytoplasm in the host cell. However, the characteristics of the nucleocytoplasmic shuttling of NP from H1N1 influenza A virus still remain unclear. In the present study, the subcellular localization and the related key residues of the H1N1 influenza virus NP were identified and evaluated...
November 8, 2016: Cellular Microbiology
https://www.readbyqxmd.com/read/27847648/increases-in-retrograde-injury-signaling-complex-related-transcripts-in-central-axons-following-injury
#5
Gunja K Pathak, Hannah Ornstein, Helim Aranda-Espinoza, Amy J Karlsson, Sameer B Shah
Axons in the peripheral nervous system respond to injury by activating retrograde injury signaling (RIS) pathways, which promote local axonal protein synthesis (LPS) and neuronal regeneration. RIS is also initiated following injury of neurons in the central nervous system (CNS). However, regulation of the localization of axonal mRNA required for LPS is not well understood. We used a hippocampal explant system to probe the regulation of axonal levels of RIS-associated transcripts following axonal injury. Axonal levels of importin β1 and RanBP1 were elevated biphasically at 1 and 24 hrs after axotomy...
2016: Neural Plasticity
https://www.readbyqxmd.com/read/27835978/importins-promote-high-frequency-nf-%C3%AE%C2%BAb-oscillations-increasing-information-channel-capacity
#6
Zbigniew Korwek, Karolina Tudelska, Paweł Nałęcz-Jawecki, Maciej Czerkies, Wiktor Prus, Joanna Markiewicz, Marek Kochańczyk, Tomasz Lipniacki
BACKGROUND: Importins and exportins influence gene expression by enabling nucleocytoplasmic shuttling of transcription factors. A key transcription factor of innate immunity, NF-κB, is sequestered in the cytoplasm by its inhibitor, IκBα, which masks nuclear localization sequence of NF-κB. In response to TNFα or LPS, IκBα is degraded, which allows importins to bind NF-κB and shepherd it across nuclear pores. NF-κB nuclear activity is terminated when newly synthesized IκBα enters the nucleus, binds NF-κB and exportin which directs the complex to the cytoplasm...
November 11, 2016: Biology Direct
https://www.readbyqxmd.com/read/27819319/nuclear-import-of-dimerized-ribosomal-protein-rps3-in-complex-with-its-chaperone-yar1
#7
Valentin Mitterer, Nadine Gantenbein, Ruth Birner-Gruenberger, Guillaume Murat, Helmut Bergler, Dieter Kressler, Brigitte Pertschy
After their cytoplasmic synthesis, ribosomal proteins need to be transported into the nucleus, where they assemble with ribosomal RNA into pre-ribosomal particles. Due to their physicochemical properties, they need protection from aggregation on this path. Newly synthesized ribosomal protein Rps3 forms a dimer that is associated with one molecule of its specific chaperone Yar1. Here we report that redundant pathways contribute to the nuclear import of Rps3, with the classical importin α/β pathway (Kap60/Kap95 in yeast) constituting a main import route...
November 7, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27816620/a-gene-delivery-system-containing-nuclear-localization-signal-increased-nucleus-import-and-transfection-efficiency-with-the-assistance-of-rangap1
#8
Kang Chen, Lingling Guo, Jiulong Zhang, Qing Chen, Kuanglei Wang, Chenxi Li, Weinan Li, Mingxi Qiao, Xiuli Zhao, Haiyang Hu, Dawei Chen
In the present report, a degradable gene delivery system (PAMS/DNA/10NLS) containing nucleus location signal peptide (NLS) was prepared. The agarose gel electrophoresis, particle size and zeta potential of PAMS/DNA/10NLS were similar to those of PAMS/DNA, which proved that NLS did not affect the interaction between PAMS and DNA. PAMS/DNA/10NLS exhibited marked extracellular and intracellular degradation under acidic conditions. The degradation was believed to allow NLS to come into contact with importins easily, which was able to mediate the nucleus import...
November 2, 2016: Acta Biomaterialia
https://www.readbyqxmd.com/read/27808165/epac1-interacts-with-importin-%C3%AE-1-and-controls-neurite-outgrowth-independently-of-camp-and-rap1
#9
Faiza Baameur, Pooja Singhmar, Yong Zhou, John F Hancock, Xiaodong Cheng, Cobi J Heijnen, Annemieke Kavelaars
Exchange protein directly activated by cAMP-1 (Epac1) is a cAMP sensor that regulates multiple cellular functions including cellular migration, proliferation and differentiation. Classically, Epac1 is thought to exert its effects through binding of cAMP leading to a conformational change in Epac1 and its accumulation at the plasma membrane (PM) where it activates Rap1. In search for regulators of Epac1 activity, we show here that importin β1 (impβ1) is an Epac1 binding partner that prevents PM accumulation of Epac1...
November 3, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27798105/effects-of-the-bowen-conradi-syndrome-mutation-in-emg1-on-its-nuclear-import-stability-and-nucleolar-recruitment
#10
Ahmed S Warda, Bernard Freytag, Sara Haag, Katherine E Sloan, Dirk Görlich, Markus T Bohnsack
Bowen-Conradi syndrome (BCS) is a severe genetic disorder that is characterised by various developmental abnormalities, bone marrow failure and early infant death. This disease is caused by a single mutation leading to the aspartate 86 to glycine (D86G) exchange in the essential nucleolar RNA methyltransferase EMG1. EMG1 is required for the synthesis of the small ribosomal subunit and is involved in modification of the 18S ribosomal RNA. Here, we identify the pre-ribosomal factors NOP14, NOC4L and UTP14A as members of a nucleolar subcomplex that contains EMG1 and is required for its recruitment to nucleoli...
October 23, 2016: Human Molecular Genetics
https://www.readbyqxmd.com/read/27794479/transportin-1-dependent-yb-1-nuclear-import
#11
Daria A Mordovkina, Ekaterina R Kim, Ilya A Buldakov, Alexey V Sorokin, Irina A Eliseeva, Dmitry N Lyabin, Lev P Ovchinnikov
The DNA/RNA-binding protein YB-1 (Y-box binding protein 1) performs multiple functions both in the cytoplasm and the nucleus of the cell. Generally localized to the cytoplasm, under certain conditions YB-1 is translocated to the nucleus. Here we report for the first time a transport factor that mediates YB-1 nuclear import - transportin-1. The YB-1/transportin-1 complex can be isolated from HeLa cell extract. Nuclear import of YB-1 and its truncated form YB-1 (1-219) in in vitro transport assay was diminished in the presence of a competitor substrate and ceased in the presence of transportin-1 inhibitor M9M...
October 26, 2016: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/27780205/stat2-is-a-pervasive-cytokine-regulator-due-to-its-inhibition-of-stat1-in-multiple-signaling-pathways
#12
Johnathan Ho, Christin Pelzel, Andreas Begitt, Maureen Mee, Hany M Elsheikha, David J Scott, Uwe Vinkemeier
STAT2 is the quintessential transcription factor for type 1 interferons (IFNs), where it functions as a heterodimer with STAT1. However, the human and murine STAT2-deficient phenotypes suggest important additional and currently unidentified type 1 IFN-independent activities. Here, we show that STAT2 constitutively bound to STAT1, but not STAT3, via a conserved interface. While this interaction was irrelevant for type 1 interferon signaling and STAT1 activation, it precluded the nuclear translocation specifically of STAT1 in response to IFN-γ, interleukin-6 (IL-6), and IL-27...
October 2016: PLoS Biology
https://www.readbyqxmd.com/read/27735996/defective-synthesis-and-release-of-astrocytic-thrombospondin-1-mediates-the-neuronal-tdp-43-proteinopathy-resulting-in-defects-in-neuronal-integrity-associated-with-chronic-traumatic-encephalopathy-in-vitro-studies
#13
A R Jayakumar, X Y Tong, N Shamaladevi, S Barcelona, G Gaidosh, A Agarwal, M D Norenberg
Transactivating DNA-binding protein-43 (TDP-43) inclusions and the accumulation of phosphorylated and ubiquitinated tau proteins (p-tau) have been identified in postmortem brain specimens from patients with chronic traumatic encephalopathy (CTE). To examine whether these proteins contribute to the development of CTE, we utilized an in vitro trauma system known to reproduce many of the findings observed in humans and experimental animals with traumatic brain injury. Accordingly, we examined the role of TDP-43 and Tau in an in vitro model of trauma, and determined whether these proteins contribute to the defective neuronal integrity associated with CNS trauma...
October 13, 2016: Journal of Neurochemistry
https://www.readbyqxmd.com/read/27733365/transcriptional-regulation-of-importin-%C3%AE-1-by-jund-modulates-subcellular-localization-of-rna-binding-protein-hur-in-intestinal-epithelial-cells
#14
Yan Xu, Jie Chen, Lan Xiao, Hee Kyoung Chung, Yuan Zhang, Joseph C Robinson, Jaladanki N Rao, Jian-Ying Wang
The RNA-binding protein HuR is crucial for normal intestinal mucosal regeneration by modulating the stability and translation of target mRNAs, but the exact mechanism underlying HuR trafficking between the cytoplasm and nucleus remains largely unknown. Here we report a novel function of transcription factor JunD in the regulation of HuR subcellular localization through the control of importin-α1 expression in intestinal epithelial cells (IECs). Ectopically expressed JunD specifically inhibited importin-α1 at the transcription level, and this repression is mediated via interaction with CREB-binding site that was located at the proximal region of importin-α1 promoter...
December 1, 2016: American Journal of Physiology. Cell Physiology
https://www.readbyqxmd.com/read/27713473/identification-of-the-nuclear-localisation-signal-of-o-glcnac-transferase-and-its-nuclear-import-regulation
#15
Hyeon Gyu Seo, Han Byeol Kim, Min Jueng Kang, Joo Hwan Ryum, Eugene C Yi, Jin Won Cho
Nucleocytoplasmic O-GlcNAc transferase (OGT) attaches a single GlcNAc to hydroxyl groups of serine and threonine residues. Although the cellular localisation of OGT is important to regulate a variety of cellular processes, the molecular mechanisms regulating the nuclear localisation of OGT is unclear. Here, we characterised three amino acids (DFP; residues 451-453) as the nuclear localisation signal of OGT and demonstrated that this motif mediated the nuclear import of non-diffusible β-galactosidase. OGT bound the importin α5 protein, and this association was abolished when the DFP motif of OGT was mutated or deleted...
October 7, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27703206/two-isoforms-of-taldo1-generated-by-alternative-translational-initiation-show-differential-nucleocytoplasmic-distribution-to-regulate-the-global-metabolic-network
#16
Tetsuji Moriyama, Shu Tanaka, Yasumune Nakayama, Masahiro Fukumoto, Kenji Tsujimura, Kohji Yamada, Takeshi Bamba, Yoshihiro Yoneda, Eiichiro Fukusaki, Masahiro Oka
Transaldolase 1 (TALDO1) is a rate-limiting enzyme involved in the pentose phosphate pathway, which is traditionally thought to occur in the cytoplasm. In this study, we found that the gene TALDO1 has two translational initiation sites, generating two isoforms that differ by the presence of the first 10 N-terminal amino acids. Notably, the long and short isoforms were differentially localised to the cell nucleus and cytoplasm, respectively. Pull-down and in vitro transport assays showed that the long isoform, unlike the short one, binds to importin α and is actively transported into the nucleus in an importin α/β-dependent manner, demonstrating that the 10 N-terminal amino acids are essential for its nuclear localisation...
October 5, 2016: Scientific Reports
https://www.readbyqxmd.com/read/27703004/quantitative-proteomics-of-the-smad-suppressor-of-mothers-against-decapentaplegic-transcription-factor-family-identifies-importin-5-as-a-bone-morphogenic-protein-receptor-smad-specific-importin
#17
Roy Baas, Ayestha Sijm, Hetty A A M van Teeffelen, Robert van Es, Harmjan R Vos, H Th Marc Timmers
Gene-specific transcription factors (GSTFs) control gene transcription by DNA binding and specific protein complex recruitment, which regulates promoter accessibility for transcription initiation by RNA polymerase II. Mutations in the GSTFs Suppressor of Mothers Against Decapentaplegic 2 (SMAD2) and SMAD4 are frequently associated with colon and rectal carcinomas. These proteins play an important role in bone morphogenic protein (BMP) and transforming growth factor β (TGF-β) signaling pathways controlling cell fate and proliferation...
November 11, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/27689332/whole-exome-sequencing-of-muscle-invasive-bladder-cancer-identifies-recurrent-copy-number-variation-in-ipo11-and-prognostic-significance-of-importin-11-overexpression-on-poor-survival
#18
Junjie Zhao, Weidong Xu, Minghui He, Zhensheng Zhang, Shuxiong Zeng, Chong Ma, Yinghao Sun, Chuanliang Xu
Non-muscle-invasive bladder cancer (NMIBC) often has a worse prognosis following its progression to muscle-invasive bladder cancer (MIBC), despite radical cystectomy with pelvic lymph node dissection combined with chemotherapy. Therefore, the discovery of novel biomarkers for predicting the progression of this disease and of therapeutic targets for preventing it is crucial. We performed whole-exome sequencing to analyze superficial tumor tissues (Tsup) and basal tumor tissues (Tbas) from 3 MIBC patients and identified previously unreported copy number variations in IPO11 that warrants further investigation as a molecular target...
September 28, 2016: Oncotarget
https://www.readbyqxmd.com/read/27677933/proteasome-dynamics-between-proliferation-and-quiescence-stages-of-saccharomyces-cerevisiae
#19
Ravikiran S Yedidi, Amatullah K Fatehi, Cordula Enenkel
The ubiquitin-proteasome system (UPS) plays a critical role in cellular protein homeostasis and is required for the turnover of short-lived and unwanted proteins, which are targeted by poly-ubiquitination for degradation. Proteasome is the key protease of UPS and consists of multiple subunits, which are organized into a catalytic core particle (CP) and a regulatory particle (RP). In Saccharomyces cerevisiae, proteasome holo-enzymes are engaged in degrading poly-ubiquitinated substrates and are mostly localized in the nucleus during cell proliferation...
September 28, 2016: Critical Reviews in Biochemistry and Molecular Biology
https://www.readbyqxmd.com/read/27669733/mechanisms-underlying-acrolein-mediated-inhibition-of-chromatin-assembly
#20
Lei Fang, Danqi Chen, Clinton Yu, Hongjie Li, Jason Brocato, Lan Huang, Chunyuan Jin
Acrolein is a major component of cigarette smoke and cooking fumes. Previously, we reported that acrolein compromises chromatin assembly; however, underlying mechanisms have not been defined. Here, we report that acrolein reacts with lysine residues, including lysines 5 and 12, sites important for chromatin assembly, on histone H4 in vitro and in vivo Acrolein-modified histones are resistant to acetylation, suggesting that the reduced H4K12 acetylation that occurs following acrolein exposure is probably due to the formation of acrolein-histone lysine adducts...
December 1, 2016: Molecular and Cellular Biology
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