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https://www.readbyqxmd.com/read/27865090/characterization-of-the-subcellular-localization-and-nuclear-import-molecular-mechanisms-of-herpes-simplex-virus-1-ul2
#1
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/27794479/transportin-1-dependent-yb-1-nuclear-import
#2
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/27618664/karyopherin-%C3%AE-2-recognition-of-a-py-nls-variant-that-lacks-the-proline-tyrosine-motif
#3
Michael Soniat, Yuh Min Chook
Karyopherin-β2 or Transportin-1 binds proline-tyrosine nuclear localization signals (PY-NLSs) in its cargos. PY-NLSs are described by structural disorder, overall positive charge, and binding epitopes composed of an N-terminal hydrophobic or basic motif and a C-terminal R-X2-5P-Y motif. The N-terminal tail of histone H3 binds Kapβ2 with high affinity but does not contain a recognizable PY-NLS. The crystal structure of the Kapβ2-H3 tail shows residues 11-27 of H3 binding to the PY-NLS site of Kapβ2. H3 residues (11)TGGKAPRK(18) bind the site for PY-NLS Epitope 1 (N-terminal hydrophobic/basic motif), which is most important for Kapβ2-binding...
October 4, 2016: Structure
https://www.readbyqxmd.com/read/27500866/the-presence-of-heterogeneous-nuclear-ribonucleoproteins-in-frontotemporal-lobar-degeneration-with-fus-positive-inclusions
#4
Priya Gami-Patel, Rina Bandopadhyay, Jack Brelstaff, Tamas Revesz, Tammaryn Lashley
Frontotemporal lobar degeneration with fused in sarcoma-positive inclusions (FTLD-FUS) is a disease with unknown cause. Transportin 1 is abundantly found in FUS-positive inclusions and responsible for the nuclear import of the FET proteins of which FUS is a member. The presence of all FET proteins in pathological inclusions suggests a disturbance of transportin 1-mediated nuclear import. FUS also belongs to the heterogeneous nuclear ribonucleoprotein (hnRNP) protein family. We investigated whether hnRNP proteins are associated with FUS pathology implicating dysfunctional nuclear export in the pathogenesis of FTLD-FUS...
October 2016: Neurobiology of Aging
https://www.readbyqxmd.com/read/27037277/phospholipid-transfer-protein-deficiency-in-mice-impairs-macrophage-reverse-cholesterol-transport-in%C3%A2-vivo
#5
Yanhong Si, Ying Zhang, Xiaofeng Chen, Lei Zhai, Guanghai Zhou, Ailing Yu, Haijun Cao, Qin Shucun
Phospholipid transfer protein is expressed in various cell types and secreted into plasma, where it transfers phospholipids between lipoproteins and modulates the composition of high-density lipoprotein particles. Phospholipid transfer protein deficiency in vivo can lower high-density lipoprotein cholesterol level significantly and impact the biological quality of high-density lipoprotein. Considering high-density lipoprotein was a critical determinant for reverse cholesterol transport, we investigated the role of systemic phospholipid transfer protein deficiency in macrophage reverse cholesterol transport in vivo After the littermate phospholipid transfer protein KO and WT mice were fed high-fat diet for one month, they were injected intraperitoneally with (3)H-cholesterol-labeled and acLDL-loaded macrophages...
July 2016: Experimental Biology and Medicine
https://www.readbyqxmd.com/read/27008858/mfsd2a-is-a-transporter-for-the-essential-%C3%AF-3-fatty-acid-docosahexaenoic-acid-dha-in-eye-and-is-important-for-photoreceptor-cell-development
#6
Bernice H Wong, Jia Pei Chan, Amaury Cazenave-Gassiot, Rebecca W Poh, Juat Chin Foo, Dwight L A Galam, Sujoy Ghosh, Long N Nguyen, Veluchamy A Barathi, Sia W Yeo, Chi D Luu, Markus R Wenk, David L Silver
Eye photoreceptor membrane discs in outer rod segments are highly enriched in the visual pigment rhodopsin and the ω-3 fatty acid docosahexaenoic acid (DHA). The eye acquires DHA from blood, but transporters for DHA uptake across the blood-retinal barrier or retinal pigment epithelium have not been identified. Mfsd2a is a newly described sodium-dependent lysophosphatidylcholine (LPC) symporter expressed at the blood-brain barrier that transports LPCs containing DHA and other long-chain fatty acids. LPC transport via Mfsd2a has been shown to be necessary for human brain growth...
May 13, 2016: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/26895297/monomethylated-and-unmethylated-fus-exhibit-increased-binding-to-transportin-and-distinguish-ftld-fus-from-als-fus
#7
Marc Suárez-Calvet, Manuela Neumann, Thomas Arzberger, Claudia Abou-Ajram, Eva Funk, Hannelore Hartmann, Dieter Edbauer, Elisabeth Kremmer, Christoph Göbl, Moritz Resch, Benjamin Bourgeois, Tobias Madl, Stefan Reber, Daniel Jutzi, Marc-David Ruepp, Ian R A Mackenzie, Olaf Ansorge, Dorothee Dormann, Christian Haass
Deposition of the nuclear DNA/RNA-binding protein Fused in sarcoma (FUS) in cytosolic inclusions is a common hallmark of some cases of frontotemporal lobar degeneration (FTLD-FUS) and amyotrophic lateral sclerosis (ALS-FUS). Whether both diseases also share common pathological mechanisms is currently unclear. Based on our previous finding that FUS deposits are hypomethylated in FTLD-FUS but not in ALS-FUS, we have now investigated whether genetic or pharmacological inactivation of Protein arginine methyltransferase 1 (PRMT1) activity results in unmethylated FUS or in alternatively methylated forms of FUS...
April 2016: Acta Neuropathologica
https://www.readbyqxmd.com/read/26854290/characterization-of-the-nuclear-import-mechanisms-of-hsv-1-ul31
#8
Mingsheng Cai, Jiang Si, Xiaowei Li, Zhancheng Zeng, Meili Li
As an important protein, UL31 has been demonstrated to play multiple roles in herpes simplex virus 1 (HSV-1) replication. Previous studies showed that UL31 predominantly locates in the nucleus in chemical fixed cells and live cells, however, the determining mechanisms for its nuclear translocation is not clear. In the present study, by utilizing live cells fluorescent microscopy and co-immunoprecipitation assays, the nuclear import of UL31 was characterized to be dependent on Ran-, importin α1- and transportin-1-mediated pathway...
June 1, 2016: Biological Chemistry
https://www.readbyqxmd.com/read/26650834/identification-of-potential-cargo-proteins-of-transportin-protein-attrn1-in-arabidopsis-thaliana
#9
Bo Yan, Xiaoning Wang, Zhenyu Wang, Ni Chen, Changjun Mu, Kaili Mao, Lirong Han, Wei Zhang, Heng Liu
We identified 23 novel proteins that can interact with At TRN1. These proteins are potential candidates of At TRN1 cargo proteins, which will facilitate our comprehending of At TRN1 functions in Arabidopsis. Tranportin 1 (TRN1) carries out the nucleo-cytoplasmic transport of many proteins, thereby ensuring that each of them is delivered to the right compartment for its proper function. These cargo proteins involved in lots of important processes, such as alternative pre-mRNA splicing, transcriptional regulation, and protein translation...
March 2016: Plant Cell Reports
https://www.readbyqxmd.com/read/26603295/treatment-with-a-global-methyltransferase-inhibitor-induces-the-intranuclear-aggregation-of-als-linked-fus-mutant-in-vitro
#10
Sakiko Fujii, Keisuke Takanashi, Keiko Kitajo, Atsushi Yamaguchi
FUS/TLS (fused in sarcoma/translocated in liposarcoma) encodes a multifunctional DNA/RNA binding protein with non-classical carboxy (C)-terminal nuclear localization signal (NLS). A variety of ALS-linked mutations are clustered in the C-terminal NLS, resulting in the cytoplasmic mislocalization and aggregation. Since the arginine methylations are implicated in the nuclear-cytoplasmic shuttling of FUS, a methylation inhibitor could be one of therapeutic targets for FUS-linked ALS. We here examined effects of methylation inhibitors on the cytoplasmic mislocalization and aggregates of ALS-linked C-terminal FUS mutant in a cell culture system...
April 2016: Neurochemical Research
https://www.readbyqxmd.com/read/26523678/structural-biology-and-regulation-of-protein-import-into-the-nucleus
#11
REVIEW
Mary Christie, Chiung-Wen Chang, Gergely Róna, Kate M Smith, Alastair G Stewart, Agnes A S Takeda, Marcos R M Fontes, Murray Stewart, Beáta G Vértessy, Jade K Forwood, Bostjan Kobe
Proteins are translated in the cytoplasm, but many need to access the nucleus to perform their functions. Understanding how these nuclear proteins are transported through the nuclear envelope and how the import processes are regulated is therefore an important aspect of understanding cell function. Structural biology has played a key role in understanding the molecular events during the transport processes and their regulation, including the recognition of nuclear targeting signals by the corresponding receptors...
May 22, 2016: Journal of Molecular Biology
https://www.readbyqxmd.com/read/26450651/identification-of-molecular-determinants-for-the-nuclear-import-of-pseudorabies-virus-ul31
#12
Meili Li, Si Jiang, Chuncong Mo, Zhancheng Zeng, Xiaowei Li, Chunke Chen, Yanjia Yang, Jinlin Wang, Jinlu Huang, Daixiong Chen, Tao Peng, Mingsheng Cai
Herpes simplex virus 1 (HSV-1) UL31 is a multifunctional protein and important for HSV-1 infection. Pseudorabies virus (PRV) UL31 is a late protein homologous to HSV-1 UL31. Previous studies showed that PRV UL31 is predominantly localized to nucleus, however, the molecular determinants for its nuclear import were unclear to date. Here, by utilizing live cells fluorescent microscopy, UL31 fused with enhanced yellow fluorescent protein was transiently expressed in live cells and confirmed to exclusively target to the nucleus in the absence of other viral proteins...
December 1, 2015: Archives of Biochemistry and Biophysics
https://www.readbyqxmd.com/read/26403203/phosphorylation-of-c-terminal-tyrosine-residue-526-in-fus-impairs-its-nuclear-import
#13
Simona Darovic, Sonja Prpar Mihevc, Vera Župunski, Gregor Gunčar, Maja Štalekar, Youn-Bok Lee, Christopher E Shaw, Boris Rogelj
Aberrant cytoplasmic aggregation of FUS, which is caused by mutations primarily in the C-terminal nuclear localisation signal, is associated with 3% of cases of familial amyotrophic lateral sclerosis (ALS). FUS aggregates are also pathognomonic for 10% of all frontotemporal lobar degeneration (FTLD) cases; however, these cases are not associated with mutations in the gene encoding FUS. This suggests that there are differences in the mechanisms that drive inclusion formation of FUS in ALS and FTLD. Here, we show that the C-terminal tyrosine residue at position 526 of FUS is crucial for normal nuclear import...
November 15, 2015: Journal of Cell Science
https://www.readbyqxmd.com/read/26324128/nuclear-export-as-a-novel-therapeutic-target-the-crm1-connection
#14
REVIEW
Chuanwen Lu, Jose A Figueroa, Zhongwei Liu, Venu Konala, Amardeep Aulakh, Rashmi Verma, Everardo Cobos, Maurizio Chiriva-Internati, Weimin Gao
The integrity of eukaryotic cellular function depends on molecular and biochemical compartmentalization. The transport of macromolecules between compartments requires specific and energydriven mechanisms. It occurs through a class of transport proteins known as karyopherins, which are divided in three different groups (exportins, importins, and transportins). The ubiquitous exportin Chromosome Region Maintenance 1 (CRM1) is involved in the transport of many proteins and RNA molecules from nucleus to cytoplasm...
2015: Current Cancer Drug Targets
https://www.readbyqxmd.com/read/26251516/sumoylation-of-the-gtpase-ran-by-the-ranbp2-sumo-e3-ligase-complex
#15
Volkan Sakin, Sebastian M Richter, He-Hsuan Hsiao, Henning Urlaub, Frauke Melchior
The SUMO E3 ligase complex RanBP2/RanGAP1*SUMO1/Ubc9 localizes at cytoplasmic nuclear pore complex (NPC) filaments and is a docking site in nucleocytoplasmic transport. RanBP2 has four Ran binding domains (RBDs), two of which flank RanBP2's E3 ligase region. We thus wondered whether the small GTPase Ran is a target for RanBP2-dependent sumoylation. Indeed, Ran is sumoylated both by a reconstituted and the endogenous RanBP2 complex in semi-permeabilized cells. Generic inhibition of SUMO isopeptidases or depletion of the SUMO isopeptidase SENP1 enhances sumoylation of Ran in semi-permeabilized cells...
September 25, 2015: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/26196321/reprint-of-nuclear-transport-factors-global-regulation-of-mitosis
#16
REVIEW
Douglass J Forbes, Anna Travesa, Matthew S Nord, Cyril Bernis
The unexpected repurposing of nuclear transport proteins from their function in interphase to an equally vital and very different set of functions in mitosis was very surprising. The multi-talented cast when first revealed included the import receptors, importin alpha and beta, the small regulatory GTPase RanGTP, and a subset of nuclear pore proteins. In this review, we report that recent years have revealed new discoveries in each area of this expanding story in vertebrates: (a) The cast of nuclear import receptors playing a role in mitotic spindle regulation has expanded: both transportin, a nuclear import receptor, and Crm1/Xpo1, an export receptor, are involved in different aspects of spindle assembly...
June 2015: Current Opinion in Cell Biology
https://www.readbyqxmd.com/read/26173234/nuclear-localization-signals-for-four-distinct-karyopherin-%C3%AE-nuclear-import-systems
#17
REVIEW
Michael Soniat, Yuh Min Chook
The Karyopherin-β family of proteins mediates nuclear transport of macromolecules. Nuclear versus cytoplasmic localization of proteins is often suggested by the presence of NLSs (nuclear localization signals) or NESs (nuclear export signals). Import-Karyopherin-βs or Importins bind to NLSs in their protein cargos to transport them through nuclear pore complexes into the nucleus. Until recently, only two classes of NLS had been biochemically and structurally characterized: the classical NLS, which is recognized by the Importin-α/β heterodimer and the PY-NLS (proline-tyrosine NLS), which is recognized by Karyopherin-β2 or Transportin-1...
June 15, 2015: Biochemical Journal
https://www.readbyqxmd.com/read/26115166/three-cardiovirus-leader-proteins-equivalently-inhibit-four-different-nucleocytoplasmic-trafficking-pathways
#18
Jessica J Ciomperlik, Holly A Basta, Ann C Palmenberg
Cardiovirus infections inhibit nucleocytoplasmic trafficking by Leader protein-induced phosphorylation of Phe/Gly-containing nucleoporins (Nups). Recombinant Leader from encephalomyocarditis virus, Theiler׳s murine encephalomyelitis virus and Saffold virus target the same subset of Nups, including Nup62 and Nup98, but not Nup50. Reporter cell lines with fluorescence mCherry markers for M9, RS and classical SV40 import pathways, as well as the Crm1-mediated export pathway, all responded to transfection with the full panel of Leader proteins, showing consequent cessation of path-specific active import/export...
October 2015: Virology
https://www.readbyqxmd.com/read/26067441/the-mammalian-cell-cycle-regulates-parvovirus-nuclear-capsid-assembly
#19
Jon Gil-Ranedo, Eva Hernando, Laura Riolobos, Carlos Domínguez, Michael Kann, José M Almendral
It is unknown whether the mammalian cell cycle could impact the assembly of viruses maturing in the nucleus. We addressed this question using MVM, a reference member of the icosahedral ssDNA nuclear parvoviruses, which requires cell proliferation to infect by mechanisms partly understood. Constitutively expressed MVM capsid subunits (VPs) accumulated in the cytoplasm of mouse and human fibroblasts synchronized at G0, G1, and G1/S transition. Upon arrest release, VPs translocated to the nucleus as cells entered S phase, at efficiencies relying on cell origin and arrest method, and immediately assembled into capsids...
June 2015: PLoS Pathogens
https://www.readbyqxmd.com/read/26060253/ipo3-mediated-nonclassical-nuclear-import-of-nf-%C3%AE%C2%BAb-essential-modulator-nemo-drives-dna-damage-dependent-nf-%C3%AE%C2%BAb-activation
#20
Byounghoon Hwang, Kevin McCool, Jun Wan, Shelly M Wuerzberger-Davis, Edmond W K Young, Eun Young Choi, Gino Cingolani, Beth A Weaver, Shigeki Miyamoto
Activation of IκB kinase (IKK) and NF-κB by genotoxic stresses modulates apoptotic responses and production of inflammatory mediators, thereby contributing to therapy resistance and premature aging. We previously reported that genotoxic agents induce nuclear localization of NF-κB essential modulator (NEMO) via an undefined mechanism to arbitrate subsequent DNA damage-dependent IKK/NF-κB signaling. Here we show that a nonclassical nuclear import pathway via IPO3 (importin 3, transportin 2) mediates stress-induced NEMO nuclear translocation...
July 17, 2015: Journal of Biological Chemistry
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