tetano
Editor, Senior Moderator
J Virol. 2012 Aug 1. [Epub ahead of print]
YB-1, Y-box binding protein-1, is a porter to lead influenza virus ribonucleoprotein complexes to microtubules.
Kawaguchi A, Matsumoto K, Nagata K.
Source
Department of Infection Biology, Faculty of Medicine and Graduate School of Comprehensive Human Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8575, Japan.
Abstract
RNA de novo synthesized are under the regulation of multiple post-transcriptional processes by a variety of RNA-binding proteins. The influenza virus genome consists of single-stranded RNAs and exists as viral ribonucleoprotein complexes (vRNP). After the replication of vRNP in the nucleus, vRNP is exported to the cytoplasm and then reaches the budding site beneath cell surface mediated by Rab11a-positive recycling endosomes along microtubules. However, the regulatory mechanisms of post-replicational 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 in vitro reconstituted systems, YB-1 was shown to be required for the interaction of nuclear-exported vRNP with microtubules around the microtubule organization 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. Taken altogether, we propose that YB-1 is a porter that leads vRNP to microtubules from the nucleus and put it on the vesicular trafficking system.
PMID:
22855482
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22855482
YB-1, Y-box binding protein-1, is a porter to lead influenza virus ribonucleoprotein complexes to microtubules.
Kawaguchi A, Matsumoto K, Nagata K.
Source
Department of Infection Biology, Faculty of Medicine and Graduate School of Comprehensive Human Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba 305-8575, Japan.
Abstract
RNA de novo synthesized are under the regulation of multiple post-transcriptional processes by a variety of RNA-binding proteins. The influenza virus genome consists of single-stranded RNAs and exists as viral ribonucleoprotein complexes (vRNP). After the replication of vRNP in the nucleus, vRNP is exported to the cytoplasm and then reaches the budding site beneath cell surface mediated by Rab11a-positive recycling endosomes along microtubules. However, the regulatory mechanisms of post-replicational 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 in vitro reconstituted systems, YB-1 was shown to be required for the interaction of nuclear-exported vRNP with microtubules around the microtubule organization 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. Taken altogether, we propose that YB-1 is a porter that leads vRNP to microtubules from the nucleus and put it on the vesicular trafficking system.
PMID:
22855482
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22855482