author_facet Kawaguchi, Atsushi
Matsumoto, Ken
Nagata, Kyosuke
Kawaguchi, Atsushi
Matsumoto, Ken
Nagata, Kyosuke
author Kawaguchi, Atsushi
Matsumoto, Ken
Nagata, Kyosuke
spellingShingle Kawaguchi, Atsushi
Matsumoto, Ken
Nagata, Kyosuke
Journal of Virology
YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
Virology
Insect Science
Immunology
Microbiology
author_sort kawaguchi, atsushi
spelling Kawaguchi, Atsushi Matsumoto, Ken Nagata, Kyosuke 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00453-12 <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>De novo</jats:italic> -synthesized RNAs are under the regulation of multiple posttranscriptional processes by a variety of RNA-binding proteins. The influenza virus genome consists of single-stranded RNAs and exists as viral ribonucleoprotein (vRNP) complexes. After the replication of vRNP in the nucleus, it is exported to the cytoplasm and then reaches the budding site beneath the cell surface in a process mediated by Rab11a-positive recycling endosomes along microtubules. However, the regulatory mechanisms of the postreplicational processes of vRNP are largely unknown. Here we identified, as a novel vRNP-interacting protein, Y-box-binding protein 1 (YB-1), a cellular protein that is involved in regulation of cellular transcription and translation. YB-1 translocated to the nucleus from the cytoplasm and accumulated in PML nuclear bodies in response to influenza virus infection. vRNP assembled into the exporting complexes with YB-1 at PML nuclear bodies. After nuclear export, using YB-1 knockdown cells and <jats:italic>in vitro</jats:italic> reconstituted systems, YB-1 was shown to be required for the interaction of vRNP exported from the nucleus with microtubules around the microtubule-organizing center (MTOC), where Rab11a-positive recycling endosomes were located. Further, we also found that YB-1 overexpression stimulates the production of progeny virions in an Rab11a-dependent manner. Taking these findings together, we propose that YB-1 is a porter that leads vRNP to microtubules from the nucleus and puts it into the vesicular trafficking system. </jats:p> YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules Journal of Virology
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title YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_unstemmed YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_full YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_fullStr YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_full_unstemmed YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_short YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_sort yb-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules
topic Virology
Insect Science
Immunology
Microbiology
url http://dx.doi.org/10.1128/jvi.00453-12
publishDate 2012
physical 11086-11095
description <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>De novo</jats:italic> -synthesized RNAs are under the regulation of multiple posttranscriptional processes by a variety of RNA-binding proteins. The influenza virus genome consists of single-stranded RNAs and exists as viral ribonucleoprotein (vRNP) complexes. After the replication of vRNP in the nucleus, it is exported to the cytoplasm and then reaches the budding site beneath the cell surface in a process mediated by Rab11a-positive recycling endosomes along microtubules. However, the regulatory mechanisms of the postreplicational processes of vRNP are largely unknown. Here we identified, as a novel vRNP-interacting protein, Y-box-binding protein 1 (YB-1), a cellular protein that is involved in regulation of cellular transcription and translation. YB-1 translocated to the nucleus from the cytoplasm and accumulated in PML nuclear bodies in response to influenza virus infection. vRNP assembled into the exporting complexes with YB-1 at PML nuclear bodies. After nuclear export, using YB-1 knockdown cells and <jats:italic>in vitro</jats:italic> reconstituted systems, YB-1 was shown to be required for the interaction of vRNP exported from the nucleus with microtubules around the microtubule-organizing center (MTOC), where Rab11a-positive recycling endosomes were located. Further, we also found that YB-1 overexpression stimulates the production of progeny virions in an Rab11a-dependent manner. Taking these findings together, we propose that YB-1 is a porter that leads vRNP to microtubules from the nucleus and puts it into the vesicular trafficking system. </jats:p>
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author Kawaguchi, Atsushi, Matsumoto, Ken, Nagata, Kyosuke
author_facet Kawaguchi, Atsushi, Matsumoto, Ken, Nagata, Kyosuke, Kawaguchi, Atsushi, Matsumoto, Ken, Nagata, Kyosuke
author_sort kawaguchi, atsushi
container_issue 20
container_start_page 11086
container_title Journal of Virology
container_volume 86
description <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>De novo</jats:italic> -synthesized RNAs are under the regulation of multiple posttranscriptional processes by a variety of RNA-binding proteins. The influenza virus genome consists of single-stranded RNAs and exists as viral ribonucleoprotein (vRNP) complexes. After the replication of vRNP in the nucleus, it is exported to the cytoplasm and then reaches the budding site beneath the cell surface in a process mediated by Rab11a-positive recycling endosomes along microtubules. However, the regulatory mechanisms of the postreplicational processes of vRNP are largely unknown. Here we identified, as a novel vRNP-interacting protein, Y-box-binding protein 1 (YB-1), a cellular protein that is involved in regulation of cellular transcription and translation. YB-1 translocated to the nucleus from the cytoplasm and accumulated in PML nuclear bodies in response to influenza virus infection. vRNP assembled into the exporting complexes with YB-1 at PML nuclear bodies. After nuclear export, using YB-1 knockdown cells and <jats:italic>in vitro</jats:italic> reconstituted systems, YB-1 was shown to be required for the interaction of vRNP exported from the nucleus with microtubules around the microtubule-organizing center (MTOC), where Rab11a-positive recycling endosomes were located. Further, we also found that YB-1 overexpression stimulates the production of progeny virions in an Rab11a-dependent manner. Taking these findings together, we propose that YB-1 is a porter that leads vRNP to microtubules from the nucleus and puts it into the vesicular trafficking system. </jats:p>
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spelling Kawaguchi, Atsushi Matsumoto, Ken Nagata, Kyosuke 0022-538X 1098-5514 American Society for Microbiology Virology Insect Science Immunology Microbiology http://dx.doi.org/10.1128/jvi.00453-12 <jats:title>ABSTRACT</jats:title> <jats:p> <jats:italic>De novo</jats:italic> -synthesized RNAs are under the regulation of multiple posttranscriptional processes by a variety of RNA-binding proteins. The influenza virus genome consists of single-stranded RNAs and exists as viral ribonucleoprotein (vRNP) complexes. After the replication of vRNP in the nucleus, it is exported to the cytoplasm and then reaches the budding site beneath the cell surface in a process mediated by Rab11a-positive recycling endosomes along microtubules. However, the regulatory mechanisms of the postreplicational processes of vRNP are largely unknown. Here we identified, as a novel vRNP-interacting protein, Y-box-binding protein 1 (YB-1), a cellular protein that is involved in regulation of cellular transcription and translation. YB-1 translocated to the nucleus from the cytoplasm and accumulated in PML nuclear bodies in response to influenza virus infection. vRNP assembled into the exporting complexes with YB-1 at PML nuclear bodies. After nuclear export, using YB-1 knockdown cells and <jats:italic>in vitro</jats:italic> reconstituted systems, YB-1 was shown to be required for the interaction of vRNP exported from the nucleus with microtubules around the microtubule-organizing center (MTOC), where Rab11a-positive recycling endosomes were located. Further, we also found that YB-1 overexpression stimulates the production of progeny virions in an Rab11a-dependent manner. Taking these findings together, we propose that YB-1 is a porter that leads vRNP to microtubules from the nucleus and puts it into the vesicular trafficking system. </jats:p> YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules Journal of Virology
spellingShingle Kawaguchi, Atsushi, Matsumoto, Ken, Nagata, Kyosuke, Journal of Virology, YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules, Virology, Insect Science, Immunology, Microbiology
title YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_full YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_fullStr YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_full_unstemmed YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_short YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
title_sort yb-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules
title_unstemmed YB-1 Functions as a Porter To Lead Influenza Virus Ribonucleoprotein Complexes to Microtubules
topic Virology, Insect Science, Immunology, Microbiology
url http://dx.doi.org/10.1128/jvi.00453-12